577:, in which an unfolded protein has a large number of conformational states available and there are fewer states available to the folded protein. A funnel implies that for protein folding there is a decrease in energy and loss of entropy with increasing tertiary structure formation. The local roughness of the funnel reflects kinetic traps, corresponding to the accumulation of misfolded intermediates. A folding chain progresses toward lower intra-chain free-energies by increasing its compactness. The chain's conformational options become increasingly narrowed ultimately toward one native structure.
669:. As the procedure does not consider the protein as a continuous chain of amino acids there are no problems in treating discontinuous domains. Specific nodes in these dendrograms are identified as tertiary structural clusters of the protein, these include both super-secondary structures and domains. The DOMAK algorithm is used to create the 3Dee domain database. It calculates a 'split value' from the number of each type of contact when the protein is divided arbitrarily into two parts. This split value is large when the two parts of the structure are distinct.
510:'palm' domain within the polymerases of the Pol I family. Since a domain can be inserted into another, there should always be at least one continuous domain in a multidomain protein. This is the main difference between definitions of structural domains and evolutionary/functional domains. An evolutionary domain will be limited to one or two connections between domains, whereas structural domains can have unlimited connections, within a given criterion of the existence of a common core. Several structural domains could be assigned to an evolutionary domain.
20:
637:
databases, especially as the number of known protein structures is increasing. Although the boundaries of a domain can be determined by visual inspection, construction of an automated method is not straightforward. Problems occur when faced with domains that are discontinuous or highly associated. The fact that there is no standard definition of what a domain really is has meant that domain assignments have varied enormously, with each researcher using a unique set of criteria.
323:, new sequences are adapted from pre-existing sequences rather than invented. Domains are the common material used by nature to generate new sequences; they can be thought of as genetically mobile units, referred to as 'modules'. Often, the C and N termini of domains are close together in space, allowing them to easily be "slotted into" parent structures during the process of evolution. Many domain families are found in all three forms of life,
991:
403:
468:
335:. Protein modules are a subset of protein domains which are found across a range of different proteins with a particularly versatile structure. Examples can be found among extracellular proteins associated with clotting, fibrinolysis, complement, the extracellular matrix, cell surface adhesion molecules and cytokine receptors. Four concrete examples of widespread protein modules are the following domains:
151:(see first figure), a glycolytic enzyme that plays an important role in regulating the flux from fructose-1,6-biphosphate to pyruvate. It contains an all-β nucleotide-binding domain (in blue), an α/β-substrate binding domain (in grey) and an α/β-regulatory domain (in olive green), connected by several polypeptide linkers. Each domain in this protein occurs in diverse sets of
722:, is publicly available in the form of a webserver. The latter allows users to optimally subdivide single-chain or multimeric proteins into quasi-rigid domains based on the collective modes of fluctuation of the system. By default the latter are calculated through an elastic network model; alternatively pre-calculated essential dynamical spaces can be uploaded by the user.
255:. Domains are the fundamental units of tertiary structure, each domain containing an individual hydrophobic core built from secondary structural units connected by loop regions. The packing of the polypeptide is usually much tighter in the interior than the exterior of the domain producing a solid-like core and a fluid-like surface. Core residues are often conserved in a
362:(PDB). However, this set contains many identical or very similar structures. All proteins should be classified to structural families to understand their evolutionary relationships. Structural comparisons are best achieved at the domain level. For this reason many algorithms have been developed to automatically assign domains in proteins with known 3D structure (see
139:
of possibilities. In a multidomain protein, each domain may fulfill its own function independently, or in a concerted manner with its neighbours. Domains can either serve as modules for building up large assemblies such as virus particles or muscle fibres, or can provide specific catalytic or binding sites as found in enzymes or regulatory proteins.
718:, that is protein regions that behave approximately as rigid units in the course of structural fluctuations, has been introduced by Potestio et al. and, among other applications was also used to compare the consistency of the dynamics-based domain subdivisions with standard structure-based ones. The method, termed
974:
using the prefix DUF followed by a number, with examples being DUF2992 and DUF1220. There are now over 3,000 DUF families within the Pfam database representing over 20% of known families. Surprisingly, the number of DUFs in Pfam has increased from 20% (in 2010) to 22% (in 2019), mostly
640:
A structural domain is a compact, globular sub-structure with more interactions within it than with the rest of the protein. Therefore, a structural domain can be determined by two visual characteristics: its compactness and its extent of isolation. Measures of local compactness in proteins have been
589:
However, the role of inter-domain interactions in protein folding and in energetics of stabilisation of the native structure, probably differs for each protein. In T4 lysozyme, the influence of one domain on the other is so strong that the entire molecule is resistant to proteolytic cleavage. In this
568:
states that if an averaged sized protein would sample all possible conformations before finding the one with the lowest energy, the whole process would take billions of years. Proteins typically fold within 0.1 and 1000 seconds. Therefore, the protein folding process must be directed some way through
560:
in the early 1960s, the goal to completely understand the mechanism by which a polypeptide rapidly folds into its stable native conformation remains elusive. Many experimental folding studies have contributed much to our understanding, but the principles that govern protein folding are still based on
506:. The kinesin motor domain can be at either end of a polypeptide chain that includes a coiled-coil region and a cargo domain. ABC transporters are built with up to four domains consisting of two unrelated modules, ATP-binding cassette and an integral membrane module, arranged in various combinations.
369:
The CATH domain database classifies domains into approximately 800 fold families; ten of these folds are highly populated and are referred to as 'super-folds'. Super-folds are defined as folds for which there are at least three structures without significant sequence similarity. The most populated is
357:
gives rise to families of related proteins with similar sequence and structure. However, sequence similarities can be extremely low between proteins that share the same structure. Protein structures may be similar because proteins have diverged from a common ancestor. Alternatively, some folds may be
657:
routine that considered proteins as several small segments, 10 residues in length. The initial segments were clustered one after another based on inter-segment distances; segments with the shortest distances were clustered and considered as single segments thereafter. The stepwise clustering finally
311:
Domain swapping is a mechanism for forming oligomeric assemblies. In domain swapping, a secondary or tertiary element of a monomeric protein is replaced by the same element of another protein. Domain swapping can range from secondary structure elements to whole structural domains. It also represents
234:
Covalent association of two domains represents a functional and structural advantage since there is an increase in stability when compared with the same structures non-covalently associated. Other, advantages are the protection of intermediates within inter-domain enzymatic clefts that may otherwise
230:
motif consists of two adjacent antiparallel β-strands joined by a small loop. It is present in most antiparallel β structures both as an isolated ribbon and as part of more complex β-sheets. Another common super-secondary structure is the β-α-β motif, which is frequently used to connect two parallel
170:
The TIM-barrel in pyruvate kinase is 'discontinuous', meaning that more than one segment of the polypeptide is required to form the domain. This is likely to be the result of the insertion of one domain into another during the protein's evolution. It has been shown from known structures that about a
166:
named after triose phosphate isomerase, which was the first such structure to be solved. It is currently classified into 26 homologous families in the CATH domain database. The TIM barrel is formed from a sequence of β-α-β motifs closed by the first and last strand hydrogen bonding together, forming
138:
Each definition is valid and will often overlap, i.e. a compact structural domain that is found amongst diverse proteins is likely to fold independently within its structural environment. Nature often brings several domains together to form multidomain and multifunctional proteins with a vast number
676:
and Janin was based on the calculated interface areas between two chain segments repeatedly cleaved at various residue positions. Interface areas were calculated by comparing surface areas of the cleaved segments with that of the native structure. Potential domain boundaries can be identified at a
572:
Advances in experimental and theoretical studies have shown that folding can be viewed in terms of energy landscapes, where folding kinetics is considered as a progressive organisation of an ensemble of partially folded structures through which a protein passes on its way to the folded structure.
636:
The importance of domains as structural building blocks and elements of evolution has brought about many automated methods for their identification and classification in proteins of known structure. Automatic procedures for reliable domain assignment is essential for the generation of the domain
593:
It has been found that the folding of an isolated domain can take place at the same rate or sometimes faster than that of the integrated domain, suggesting that unfavourable interactions with the rest of the protein can occur during folding. Several arguments suggest that the slowest step in the
509:
Not only do domains recombine, but there are many examples of a domain having been inserted into another. Sequence or structural similarities to other domains demonstrate that homologues of inserted and parent domains can exist independently. An example is that of the 'fingers' inserted into the
487:
comprises about 120 fibronectin-III-type and Ig-type domains. In the serine proteases, a gene duplication event has led to the formation of a two β-barrel domain enzyme. The repeats have diverged so widely that there is no obvious sequence similarity between them. The active site is located at a
290:
Domains have limits on size. The size of individual structural domains varies from 36 residues in E-selectin to 692 residues in lipoxygenase-1, but the majority, 90%, have fewer than 200 residues with an average of approximately 100 residues. Very short domains, less than 40 residues, are often
513:
A superdomain consists of two or more conserved domains of nominally independent origin, but subsequently inherited as a single structural/functional unit. This combined superdomain can occur in diverse proteins that are not related by gene duplication alone. An example of a superdomain is the
193:
ultimately encodes its uniquely folded three-dimensional (3D) conformation. The most important factor governing the folding of a protein into 3D structure is the distribution of polar and non-polar side chains. Folding is driven by the burial of hydrophobic side chains into the interior of the
585:
The organisation of large proteins by structural domains represents an advantage for protein folding, with each domain being able to individually fold, accelerating the folding process and reducing a potentially large combination of residue interactions. Furthermore, given the observed random
911:
have all been observed. Given the fact that phosphoinositides are sequestered to various cell membranes (due to their long lipophilic tail) the PH domains usually causes recruitment of the protein in question to a membrane where the protein can exert a certain function in cell signalling,
395:
domains (GARs-AIRs-GARt; GAR: glycinamide ribonucleotide synthetase/transferase; AIR: aminoimidazole ribonucleotide synthetase). In insects, the polypeptide appears as GARs-(AIRs)2-GARt, in yeast GARs-AIRs is encoded separately from GARt, and in bacteria each domain is encoded separately.
167:
an eight stranded barrel. There is debate about the evolutionary origin of this domain. One study has suggested that a single ancestral enzyme could have diverged into several families, while another suggests that a stable TIM-barrel structure has evolved through convergent evolution.
594:
folding of large proteins is the pairing of the folded domains. This is either because the domains are not folded entirely correctly or because the small adjustments required for their interaction are energetically unfavourable, such as the removal of water from the domain interface.
303:, which consists of several polypeptide chains that associate into an oligomeric molecule. Each polypeptide chain in such a protein is called a subunit. Hemoglobin, for example, consists of two α and two β subunits. Each of the four chains has an all-α globin fold with a heme pocket.
680:
The PUU algorithm incorporates a harmonic model used to approximate inter-domain dynamics. The underlying physical concept is that many rigid interactions will occur within each domain and loose interactions will occur between domains. This algorithm is used to define domains in the
198:
surrounded by a shell of hydrophilic residues. Since the peptide bonds themselves are polar they are neutralised by hydrogen bonding with each other when in the hydrophobic environment. This gives rise to regions of the polypeptide that form regular 3D structural patterns called
688:
Swindells (1995) developed a method, DETECTIVE, for identification of domains in protein structures based on the idea that domains have a hydrophobic interior. Deficiencies were found to occur when hydrophobic cores from different domains continue through the interface region.
378:
The majority of proteins, two-thirds in unicellular organisms and more than 80% in metazoa, are multidomain proteins. However, other studies concluded that 40% of prokaryotic proteins consist of multiple domains while eukaryotes have approximately 65% multi-domain proteins.
358:
more favored than others as they represent stable arrangements of secondary structures and some proteins may converge towards these folds over the course of evolution. There are currently about 110,000 experimentally determined protein 3D structures deposited within the
865:(PTB): PTB domains usually bind to phosphorylated tyrosine residues. They are often found in signal transduction proteins. PTB-domain binding specificity is determined by residues to the amino-terminal side of the phosphotyrosine. Examples: the PTB domains of both
382:
Many domains in eukaryotic multidomain proteins can be found as independent proteins in prokaryotes, suggesting that domains in multidomain proteins have once existed as independent proteins. For example, vertebrates have a multi-enzyme polypeptide containing the
270:
All-β domains have a core composed of antiparallel β-sheets, usually two sheets packed against each other. Various patterns can be identified in the arrangement of the strands, often giving rise to the identification of recurring motifs, for example the Greek key
437:
to create new functions. Various proteins have diverged from common ancestors by different combinations and associations of domains. Modular units frequently move about, within and between biological systems through mechanisms of genetic shuffling:
402:
1757:
Banner DW, Bloomer AC, Petsko GA, Phillips DC, Pogson CI, Wilson IA, et al. (June 1975). "Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data".
231:β-strands. The central α-helix connects the C-termini of the first strand to the N-termini of the second strand, packing its side chains against the β-sheet and therefore shielding the hydrophobic residues of the β-strands from the surface.
590:
case, folding is a sequential process where the C-terminal domain is required to fold independently in an early step, and the other domain requires the presence of the folded C-terminal domain for folding and stabilisation.
695:
is a novel method for identification of protein rigid blocks (domains and loops) from two different conformations. Rigid blocks are defined as blocks where all inter residue distances are conserved across conformations.
620:. The resultant dynamic modes cannot be generally predicted from static structures of either the entire protein or individual domains. They can however be inferred by comparing different structures of a protein (as in
586:
distribution of hydrophobic residues in proteins, domain formation appears to be the optimal solution for a large protein to bury its hydrophobic residues while keeping the hydrophilic residues at the surface.
5156:, Sayre JR, Merutka G, Shin HC, Lerner RA, Wright PE (August 1992). "Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. II. Plastocyanin".
534:
and the membrane protein TPTE2. This superdomain is found in proteins in animals, plants and fungi. A key feature of the PTP-C2 superdomain is amino acid residue conservation in the domain interface.
561:
those discovered in the very first studies of folding. Anfinsen showed that the native state of a protein is thermodynamically stable, the conformation being at a global minimum of its free energy.
281:α/β domains are made from a combination of β-α-β motifs that predominantly form a parallel β-sheet surrounded by amphipathic α-helices. The secondary structures are arranged in layers or barrels.
918:(SH2): SH2 domains are often found in signal transduction proteins. SH2 domains confer binding to phosphorylated tyrosine (pTyr). Named after the phosphotyrosine binding domain of the src viral
495:
were shown to have some proteinase activity even though their active site residues were abolished and it has therefore been postulated that the duplication event enhanced the enzyme's activity.
274:α+β domains are a mixture of all-α and all-β motifs. Classification of proteins into this class is difficult because of overlaps to the other three classes and therefore is not used in the
68:
uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50
4862:
Micheletti, C., Carloni, P. and
Maritan, A. Accurate and efficient description of protein vibrational dynamics: comparing molecular dynamics and gaussian models, Proteins, 55, 635, 2004.
3207:
Politou AS, Gautel M, Improta S, Vangelista L, Pastore A (February 1996). "The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains".
569:
a specific folding pathway. The forces that direct this search are likely to be a combination of local and global influences whose effects are felt at various stages of the reaction.
624:). They can also be suggested by sampling in extensive molecular dynamics trajectories and principal component analysis, or they can be directly observed using spectra measured by
267:
All-α domains have a domain core built exclusively from α-helices. This class is dominated by small folds, many of which form a simple bundle with helices running up and down.
251:
Several motifs pack together to form compact, local, semi-independent units called domains. The overall 3D structure of the polypeptide chain is referred to as the protein's
650:
2220:
Zhou Y, Vitkup D, Karplus M (January 1999). "Native proteins are surface-molten solids: application of the
Lindemann criterion for the solid versus liquid state".
2914:
Ekman D, Björklund AK, Frey-Skött J, Elofsson A (April 2005). "Multi-domain proteins in the three kingdoms of life: orphan domains and other unassigned regions".
665:
The method by
Sowdhamini and Blundell clusters secondary structures in a protein based on their Cα-Cα distances and identifies domains from the pattern in their
259:, whereas the residues in loops are less conserved, unless they are involved in the protein's function. Protein tertiary structure can be divided into four main
608:
Protein domain dynamics play a key role in a multitude of molecular recognition and signaling processes. Protein domains, connected by intrinsically disordered
839:
and are classified into different categories (IgV, IgC1, IgC2 and IgI) according to their size and function. They possess a characteristic fold in which two
659:
6387:
1712:
Hegyi H, Gerstein M (April 1999). "The relationship between protein structure and function: a comprehensive survey with application to the yeast genome".
751:
proteins. One part of the domain contains a region that mediates sequence-specific DNA-binding properties and the
Leucine zipper that is required for the
260:
488:
cleft between the two β-barrel domains, in which functionally important residues are contributed from each domain. Genetically engineered mutants of the
790:
via proteolytic cascades. Pro-caspase-8 and pro-caspase-9 bind to specific adaptor molecules via DED domains, which leads to autoactivation of caspases.
2949:
Davidson JN, Chen KC, Jamison RS, Musmanno LA, Kern CB (March 1993). "The evolutionary history of the first three enzymes in pyrimidine biosynthesis".
3408:
773:
proteins. Cadherin domains are extracellular regions which mediate cell-to-cell homophilic binding between cadherins on the surface of adjacent cells.
171:
quarter of structural domains are discontinuous. The inserted β-barrel regulatory domain is 'continuous', made up of a single stretch of polypeptide.
6795:
2992:
Henikoff S, Greene EA, Pietrokovski S, Bork P, Attwood TK, Hood L (October 1997). "Gene families: the taxonomy of protein paralogs and chimeras".
662:
were represented as diagonal plots in which there were distinct patterns for helices, extended strands and combinations of secondary structures.
658:
included the full protein. Go also exploited the fact that inter-domain distances are normally larger than intra-domain distances; all possible
479:
The simplest multidomain organization seen in proteins is that of a single domain repeated in tandem. The domains may interact with each other (
2775:
312:
a model of evolution for functional adaptation by oligomerisation, e.g. oligomeric enzymes that have their active site at subunit interfaces.
291:
stabilised by metal ions or disulfide bonds. Larger domains, greater than 300 residues, are likely to consist of multiple hydrophobic cores.
235:
be unstable in aqueous environments, and a fixed stoichiometric ratio of the enzymatic activity necessary for a sequential set of reactions.
896:
1351:
5355:
4776:
Pandurangan AP, Topf M (February 2012). "Finding rigid bodies in protein structures: Application to flexible fitting into cryoEM maps".
1894:
Lesk AM, Brändén CI, Chothia C (1989). "Structural principles of alpha/beta barrel proteins: the packing of the interior of the sheet".
6012:
Library of HMMs representing superfamilies and database of (superfamily and family) annotations for all completely sequenced organisms
5532:
970: (DUF) is a protein domain that has no characterized function. These families have been collected together in the
6050:
3609:"Statistical distribution of hydrophobic residues along the length of protein chains. Implications for protein folding and evolution"
682:
162:
folds. It is seen in many different enzyme families catalysing completely unrelated reactions. The α/β-barrel is commonly called the
677:
site where the interface area was at a minimum. Other methods have used measures of solvent accessibility to calculate compactness.
6608:
6380:
415:
Attractin-like protein 1 (ATRNL1) is a multi-domain protein found in animals, including humans. Each unit is one domain, e.g. the
3045:
Walker WP, Aradhya S, Hu CL, Shen S, Zhang W, Azarani A, et al. (December 2007). "Genetic analysis of attractin homologs".
6247:
4872:
Barclay AN (August 2003). "Membrane proteins with immunoglobulin-like domains--a master superfamily of interaction molecules".
1106:
George, R. A. (2002) "Predicting
Structural Domains in Proteins" Thesis, University College London (contributed by its author).
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Folding is a directed search of conformational space allowing the protein to fold on a biologically feasible time scale. The
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6788:
5879:"SUPERFAMILY: HMMs representing all proteins of known structure. SCOP sequence searches, alignments and genome assignments"
6373:
6297:
3854:"Coarse-grained description of protein internal dynamics: an optimal strategy for decomposing proteins in rigid subunits"
3664:
George RA, Heringa J (February 2002). "SnapDRAGON: a method to delineate protein structural domains from sequence data".
4736:"RIBFIND: a web server for identifying rigid bodies in protein structures and to aid flexible fitting into cryo EM maps"
4518:"Continuous and discontinuous domains: an algorithm for the automatic generation of reliable protein domain definitions"
2351:"Proteins of Escherichia coli come in sizes that are multiples of 14 kDa: domain concepts and evolutionary implications"
617:
603:
2658:"The conservation pattern of short linear motifs is highly correlated with the function of interacting protein domains"
384:
4089:"An automatic method involving cluster analysis of secondary structures for the identification of domains in proteins"
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6888:
6840:
6242:
2751:
2176:
1375:
2871:
Apic G, Gough J, Teichmann SA (July 2001). "Domain combinations in archaeal, eubacterial and eukaryotic proteomes".
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developed by
Pandurangan and Topf identifies rigid bodies in protein structures by performing spacial clustering of
6878:
866:
6883:
6781:
6636:
6257:
7002:
6165:
5379:
Heringa J, Argos P (July 1991). "Side-chain clusters in protein structures and their role in protein folding".
4313:
Rossmann MG, Moras D, Olsen KW (July 1974). "Chemical and biological evolution of nucleotide-binding protein".
862:
4567:"Identification of compact, hydrophobically stabilized domains and modules containing multiple peptide chains"
3795:"Antibody as immunological probe for studying refolding of bovine serum albumin. Refolding within each domain"
2492:
Garel, J. (1992). "Folding of large proteins: Multidomain and multisubunit proteins". In
Creighton, T. (ed.).
855:, cell activation, and molecular recognition. These domains are commonly found in molecules with roles in the
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6043:
5952:
2602:
719:
708:
621:
1688:"Protein Domains, Domain Assignment, Identification and Classification According to CATH and SCOP Databases"
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6835:
6601:
5979:
3439:
1036:
515:
300:
5533:"SCOP: a structural classification of proteins database for the investigation of sequences and structures"
6908:
6825:
3758:
Desmadril M, Yon JM (July 1981). "Existence of intermediates in the refolding of T4 lysozyme at pH 7.4".
2314:
Hutchinson EG, Thornton JM (April 1993). "The Greek key motif: extraction, classification and analysis".
1687:
1009:
704:
344:
200:
194:
molecule so to avoid contact with the aqueous environment. Generally proteins have a core of hydrophobic
3280:
Moore JD, Endow SA (March 1996). "Kinesin proteins: a phylum of motors for microtubule-based motility".
64:. Many proteins consist of several domains, and a domain may appear in a variety of different proteins.
6987:
6830:
6396:
6309:
5728:
Tatusov RL, Natale DA, Garkavtsev IV, Tatusova TA, Shankavaram UT, Rao BS, et al. (January 2001).
961:
884:
832:
472:
252:
61:
6997:
6964:
6820:
5730:"The COG database: new developments in phylogenetic classification of proteins from complete genomes"
5656:
Siddiqui AS, Dengler U, Barton GJ (February 2001). "3Dee: a database of protein structural domains".
3970:"Activation of nanoscale allosteric protein domain motion revealed by neutron spin echo spectroscopy"
186:
5478:"The SBASE protein domain library, release 7.0: a collection of annotated protein sequence segments"
3678:
3014:
2206:
2040:"The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain"
1942:"Domain assignment for protein structures using a consensus approach: characterization and analysis"
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6992:
6036:
5870:
5422:
5262:
Go M (May 1981). "Correlation of DNA exonic regions with protein structural units in haemoglobin".
448:
219:
5112:"A fully automatic evolutionary classification of protein folds: Dali Domain Dictionary version 3"
2707:
Campbell ID, Downing AK (May 1994). "Building protein structure and function from modular units".
755:
of two DNA-binding regions. The DNA-binding region comprises a number of basic aminoacids such as
641:
used in many of the early methods of domain assignment and in several of the more recent methods.
6594:
5217:
George DG, Hunt LT, Barker WC (1996). "[3] PIR-International protein sequence database".
3911:"LSD1/CoREST is an allosteric nanoscale clamp regulated by H3-histone-tail molecular recognition"
2820:
Orengo CA, Jones DT, Thornton JM (December 1994). "Protein superfamilies and domain superfolds".
2790:
2566:
Heringa J, Taylor WR (June 1997). "Three-dimensional domain duplication, swapping and stealing".
2413:
Islam SA, Luo J, Sternberg MJ (June 1995). "Identification and analysis of domains in proteins".
736:
654:
5575:
2097:
Cordes MH, Davidson AR, Sauer RT (February 1996). "Sequence space, folding and protein design".
214:
Some simple combinations of secondary structure elements have been found to frequently occur in
6865:
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5417:
5408:
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Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, et al. (January 2000).
4956:
El-Gebali S, Mistry J, Bateman A, Eddy SR, Luciani A, Potter SC, et al. (January 2019).
4228:"Hydrophobic folding units derived from dissimilar monomer structures and their interactions"
1855:"Homology among (betaalpha)(8) barrels: implications for the evolution of metabolic pathways"
915:
776:
707:
in proteins. The RIBFIND rigid bodies have been used to flexibly fit protein structures into
613:
557:
340:
6025:
A comprehensive database of domain-centric ontologies on functions, phenotypes and diseases.
4027:"Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy"
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Drenth J, Jansonius JN, Koekoek R, Swen HM, Wolthers BG (June 1968). "Structure of papain".
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5837:"Free energy determinants of secondary structure formation: II. Antiparallel beta-sheets"
1648:"An analysis of protein domain linkers: their classification and role in protein folding"
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3969:
3945:
3910:
3886:
3853:
3735:
3710:
3641:
3608:
3589:
3482:
3457:
3384:
3359:
3305:
3070:
2974:
2896:
2853:
2769:
2684:
2657:
2638:
2543:
2518:
2296:
2245:
2194:
2017:
1966:
1941:
1919:
1791:
1623:
1588:
1569:
1450:
1243:
1192:
1073:
1068:
948:
940:
498:
Modules frequently display different connectivity relationships, as illustrated by the
392:
5711:
5686:
5669:
5639:
5614:
5551:
5502:
5477:
5325:
5308:
5245:
5226:
5201:
5084:
5035:
5010:
4885:
4490:
4465:
4438:
4403:
3811:
3794:
3632:
3185:
2579:
2466:
2449:
2385:
2350:
2168:
2159:
Ostermeier M, Benkovic SJ (2000). "Evolution of protein function by domain swapping".
2110:
2074:
2039:
1830:
1813:
1504:
1469:
1367:
1180:
1159:
Phillips DC (November 1966). "The three-dimensional structure of an enzyme molecule".
1136:
1119:
6812:
6672:
6646:
6528:
6420:
6344:
5908:
5903:
5878:
5858:
5823:
5788:
5784:
5759:
5754:
5729:
5716:
5685:
Srinivasarao GY, Yeh LS, Marzec CR, Orcutt BC, Barker WC, Pfeiffer F (January 1999).
5673:
5644:
5601:
5591:
5587:
5555:
5520:
5507:
5464:
5435:
5396:
5392:
5359:
5330:
5287:
5250:
5230:
5205:
5173:
5169:
5141:
5136:
5111:
5098:
5088:
5057:
5040:
4987:
4938:
4889:
4837:
4793:
4758:
4716:
4672:
4637:
4596:
4547:
4495:
4443:
4381:
4377:
4338:
4295:
4291:
4257:
4208:
4203:
4186:
4167:
4118:
4066:
4007:
3950:
3891:
3816:
3775:
3771:
3740:
3691:
3646:
3581:
3546:
3541:
3506:
3487:
3389:
3340:
3297:
3262:
3258:
3224:
3189:
3154:
3149:
3114:
3062:
3027:
2966:
2931:
2888:
2845:
2757:
2747:
2724:
2720:
2689:
2630:
2583:
2548:
2497:
2471:
2430:
2390:
2331:
2288:
2237:
2182:
2172:
2141:
2114:
2079:
2009:
1971:
1911:
1876:
1835:
1783:
1739:
1669:
1628:
1561:
1509:
1442:
1437:
1412:
1381:
1371:
1329:
1286:
1235:
1184:
1141:
1061:
1031:
1014:
808:
804:
731:
625:
565:
359:
215:
180:
121:
93:
41:
28:
5947:
5932:
5371:
4849:
4832:
4815:
4754:
4364:
Rose GD (November 1979). "Hierarchic organization of domains in globular proteins".
3593:
3507:"Protein folding funnels: a kinetic approach to the sequence-structure relationship"
3309:
3074:
2978:
2900:
2642:
1923:
1454:
1196:
483:) or remain isolated, like beads on string. The giant 30,000 residue muscle protein
445:
gross rearrangements such as inversions, translocations, deletions and duplications;
108:
was first proposed in 1973 by
Wetlaufer after X-ray crystallographic studies of hen
6959:
6750:
6708:
6703:
6698:
6523:
6446:
6334:
5898:
5890:
5848:
5813:
5780:
5749:
5741:
5706:
5698:
5665:
5634:
5626:
5583:
5547:
5497:
5489:
5456:
5427:
5388:
5351:
5320:
5309:"A systematic comparison of protein structure classifications: SCOP, CATH and FSSP"
5299:
5279:
5240:
5222:
5197:
5165:
5131:
5123:
5080:
5030:
5022:
4977:
4969:
4928:
4920:
4881:
4827:
4785:
4750:
4708:
4664:
4627:
4586:
4578:
4537:
4529:
4485:
4477:
4433:
4423:
4373:
4350:
4330:
4287:
4247:
4239:
4198:
4187:"Structural domains in proteins and their role in the dynamics of protein function"
4157:
4149:
4108:
4100:
4056:
4046:
3997:
3989:
3940:
3930:
3881:
3873:
3806:
3767:
3730:
3722:
3683:
3636:
3628:
3573:
3536:
3526:
3477:
3469:
3431:
3379:
3371:
3332:
3289:
3254:
3216:
3181:
3144:
3134:
3054:
3019:
2958:
2923:
2880:
2857:
2837:
2716:
2679:
2669:
2622:
2575:
2538:
2530:
2461:
2422:
2380:
2370:
2323:
2300:
2280:
2249:
2229:
2164:
2106:
2069:
2059:
2001:
1961:
1953:
1940:
Jones S, Stewart M, Michie A, Swindells MB, Orengo C, Thornton JM (February 1998).
1903:
1866:
1825:
1795:
1775:
1731:
1659:
1618:
1608:
1573:
1551:
1499:
1489:
1432:
1363:
1321:
1278:
1247:
1227:
1176:
1131:
1094:
888:
825:
800:
797:
503:
223:
152:
124:
that could fold autonomously. In the past domains have been described as units of:
4816:"PiSQRD: a web server for decomposing proteins into quasi-rigid dynamical domains"
2021:
1812:
Orengo CA, Michie AD, Jones S, Jones DT, Swindells MB, Thornton JM (August 1997).
442:
transposition of mobile elements including horizontal transfers (between species);
19:
6656:
6641:
6549:
6513:
6415:
5956:
3023:
1613:
1325:
1282:
923:
908:
609:
548:
492:
480:
416:
148:
117:
57:
23:
4655:
Wodak SJ, Janin J (November 1981). "Location of structural domains in protein".
3336:
1664:
1647:
6850:
6554:
6482:
6451:
6272:
6135:
4632:
4615:
4408:
Proceedings of the
National Academy of Sciences of the United States of America
4031:
Proceedings of the National Academy of Sciences of the United States of America
3915:
Proceedings of the National Academy of Sciences of the United States of America
3511:
Proceedings of the National Academy of Sciences of the United States of America
3119:
Proceedings of the National Academy of Sciences of the United States of America
2355:
Proceedings of the National Academy of Sciences of the United States of America
2044:
Proceedings of the National Academy of Sciences of the United States of America
1474:
Proceedings of the National Academy of Sciences of the United States of America
1089:
1056:
1004:
996:
673:
574:
455:
433:
Multidomain proteins are likely to have emerged from selective pressure during
388:
348:
256:
77:
4924:
4789:
3993:
3877:
3172:
Heringa J (June 1998). "Detection of internal repeats: how common are they?".
2927:
2426:
2327:
16:
Self-stable region of a protein's chain that folds independently from the rest
6981:
6735:
6730:
6518:
6365:
6205:
5874:
5802:"Free energy determinants of secondary structure formation: I. alpha-Helices"
5528:
4814:
Aleksiev T, Potestio R, Pontiggia F, Cozzini S, Micheletti C (October 2009).
3435:
2761:
2263:
Levitt M, Chothia C (June 1976). "Structural patterns in globular proteins".
1527:
1084:
904:
900:
856:
852:
821:
770:
752:
420:
4735:
4278:
Crippen GM (December 1978). "The tree structural organization of proteins".
4051:
3935:
3531:
3139:
2674:
6944:
6436:
6287:
6210:
6195:
6155:
6090:
5912:
5894:
5853:
5836:
5818:
5801:
5763:
5702:
5677:
5648:
5630:
5511:
5493:
5439:
5431:
5363:
5356:
10.1002/(SICI)1097-0134(19990901)36:4<425::AID-PROT6>3.0.CO;2-S
5334:
5145:
5102:
5044:
5026:
4991:
4942:
4893:
4841:
4797:
4762:
4641:
4582:
4533:
4481:
4404:"Respective roles of short- and long-range interactions in protein folding"
4243:
4153:
4104:
4070:
4011:
3954:
3895:
3744:
3695:
3687:
3491:
3393:
3293:
3220:
3066:
2962:
2935:
2892:
2884:
2693:
2626:
2534:
2475:
2375:
2233:
2186:
2083:
2064:
2005:
1957:
1907:
1880:
1871:
1854:
1743:
1735:
1673:
1632:
779:(DED): allows protein–protein binding by homotypic interactions (DED-DED).
489:
73:
5862:
5827:
5792:
5745:
5720:
5605:
5559:
5468:
5400:
5291:
5254:
5209:
5177:
5127:
5110:
Dietmann S, Park J, Notredame C, Heger A, Lappe M, Holm L (January 2001).
4720:
4676:
4600:
4551:
4499:
4428:
4342:
4261:
4212:
4171:
4122:
3779:
3650:
3585:
3564:
Dill KA, Chan HS (January 1997). "From Levinthal to pathways to funnels".
3550:
3344:
3301:
3228:
3193:
3158:
3031:
2970:
2849:
2728:
2587:
2552:
2434:
2394:
2335:
2241:
2118:
2013:
1975:
1915:
1839:
1787:
1565:
1513:
1494:
1446:
1385:
1333:
1290:
1239:
1188:
1145:
877:
sequence. PTB-containing proteins such as SHC and IRS-1 are important for
227:
158:
The central α/β-barrel substrate binding domain is one of the most common
6773:
6755:
6745:
6477:
6441:
6354:
6339:
6262:
6252:
6232:
6227:
6222:
6185:
6140:
6115:
6100:
6095:
6080:
5524:
5185:
4973:
4447:
4385:
4299:
3820:
3726:
3266:
2634:
2292:
2145:
937:
744:
523:
204:
5937:
4712:
4668:
3473:
2496:(First ed.). New York: W.H. Freeman and Company. pp. 405–454.
1470:"Nucleation, rapid folding, and globular intrachain regions in proteins"
6939:
6682:
6559:
6503:
6487:
6456:
6329:
6324:
6319:
6304:
6292:
6277:
6217:
6190:
6180:
6175:
6170:
6160:
6130:
6125:
6110:
6105:
6085:
6075:
5576:"Domains in proteins: definitions, location, and structural principles"
5476:
Murvai J, Vlahovicek K, Barta E, Cataletto B, Pongor S (January 2000).
5153:
3577:
931:
892:
848:
843:
form a "sandwich" that is stabilized by interactions between conserved
840:
836:
815:
811:
666:
336:
208:
163:
85:
69:
4025:
Bu Z, Biehl R, Monkenbusch M, Richter D, Callaway DJ (December 2005).
3058:
1304:
Edelman GM (May 1973). "Antibody structure and molecular immunology".
851:. They are important for protein–protein interactions in processes of
32:
6760:
6575:
6544:
6314:
6237:
6150:
6145:
6070:
6022:
5615:"SMART: a web-based tool for the study of genetically mobile domains"
5283:
4334:
3375:
3360:"Superdomains in the protein structure hierarchy: The case of PTP-C2"
2841:
2284:
1779:
1556:
1531:
1231:
787:
748:
519:
434:
88:. Because they are independently stable, domains can be "swapped" by
734:: named after the β-catenin-like Armadillo protein of the fruit fly
6713:
6651:
6004:
5962:
5613:
Schultz J, Copley RR, Doerks T, Ponting CP, Bork P (January 2000).
3711:"Scooby-domain: prediction of globular domains in protein sequence"
990:
919:
844:
783:
766:
756:
363:
328:
109:
80:. Domains often form functional units, such as the calcium-binding
6028:
5999:
5933:
Conserved Domains at the National Center for Biotechnology website
4699:
Zehfus MH, Rose GD (September 1986). "Compact units in proteins".
1992:
Holm L, Sander C (July 1994). "Parser for protein folding units".
692:
467:
6924:
6723:
6718:
6617:
5989:
5771:
Taylor WR, Orengo CA (July 1989). "Protein structure alignment".
5071:
Das S, Smith TF (2000). "Identifying nature's protein Lego set".
3968:
Farago B, Li J, Cornilescu G, Callaway DJ, Bu Z (November 2010).
1026:
878:
793:
780:
631:
531:
499:
332:
324:
190:
81:
53:
49:
6009:
5974:
4813:
2913:
1814:"CATH--a hierarchic classification of protein domain structures"
1586:
700:
60:
independently from the rest. Each domain forms a compact folded
5727:
2163:. Advances in Protein Chemistry. Vol. 55. pp. 29–77.
1261:
Porter RR (May 1973). "Structural studies of immunoglobulins".
976:
760:
527:
159:
113:
72:
up to 250 amino acids in length. The shortest domains, such as
5475:
3206:
3115:"Proposed acquisition of an animal protein domain by bacteria"
2991:
1589:"The crystal structure of Toxoplasma gondii pyruvate kinase 1"
943:(ZnF_GATA): ZnF_GATA domain-containing proteins are typically
5188:(February 1997). "Nucleation mechanisms in protein folding".
4466:"Dali/FSSP classification of three-dimensional protein folds"
1532:"Proteins. One thousand families for the molecular biologist"
874:
870:
484:
5008:
966:
A large fraction of domains are of unknown function. A
604:
Protein dynamics § Global flexibility: multiple domains
6586:
5953:
Definition and assignment of structural domains in proteins
5684:
5518:
3851:
2948:
2516:
2447:
1939:
1756:
1020:
971:
275:
5942:
5612:
5109:
4955:
4138:"A procedure for detecting structural domains in proteins"
3967:
2656:
Ren S, Yang G, He Y, Wang Y, Li Y, Chen Z (October 2008).
1209:
580:
6954:
6949:
5994:
5582:. Methods in Enzymology. Vol. 115. pp. 420–30.
4024:
2517:
Bennett MJ, Schlunegger MP, Eisenberg D (December 1995).
2450:"Domain size distributions can predict domain boundaries"
2038:
Anfinsen CB, Haber E, Sela M, White FH (September 1961).
263:
based on the secondary structural content of the domain.
5580:
Diffraction Methods for Biological Macromolecules Part B
5221:. Methods in Enzymology. Vol. 266. pp. 41–59.
3088:
2519:"3D domain swapping: a mechanism for oligomer assembly"
537:
2798:
2037:
1811:
831:
Immunoglobulin-like domains: found in proteins of the
769:
repeats: Cadherins function as Ca-dependent cell–cell
5655:
5152:
2448:
Wheelan SJ, Marchler-Bauer A, Bryant SH (July 2000).
364:§ Domain definition from structural co-ordinates
3504:
986:
912:
cytoskeletal reorganization or membrane trafficking.
370:
the α/β-barrel super-fold, as described previously.
3852:Potestio R, Pontiggia F, Micheletti C (June 2009).
3760:
Biochemical and Biophysical Research Communications
3505:Leopold PE, Montal M, Onuchic JN (September 1992).
3044:
2819:
2096:
203:. There are two main types of secondary structure:
5687:"Database of protein sequence alignments: PIR-ALN"
4906:
4312:
4086:
2870:
2313:
2158:
2134:Comptes Rendus de l'Académie des Sciences, Série D
1893:
597:
315:
4082:
4080:
3847:
3845:
3843:
3240:
3238:
2412:
2219:
1345:
1343:
979:. Pfam release 32.0 (2019) contained 3,961 DUFs.
6979:
5216:
4809:
4807:
3708:
3323:Russell RB (December 1994). "Domain insertion".
2649:
2033:
2031:
1017:, a biological database covering protein domains
4775:
4733:
4511:
4509:
4273:
4271:
2706:
1352:"The anatomy and taxonomy of protein structure"
120:. Wetlaufer defined domains as stable units of
6395:
6016:
5926:
4907:Bateman A, Coggill P, Finn RD (October 2010).
4515:
4077:
3840:
3235:
1340:
1085:CATH Protein Structure Classification database
955:
947:that usually bind to the DNA sequence GATA of
632:Domain definition from structural co-ordinates
241:is an important tool for determining domains.
6789:
6602:
6381:
6044:
4804:
4129:
3835:Proteins: Structures and molecular properties
3792:
3663:
3400:
3112:
2655:
2565:
2262:
2028:
1807:
1805:
1711:
1645:
475:modules (maroon) into two different proteins.
174:
5968:
5869:
5770:
5573:
5378:
5051:
4958:"The Pfam protein families database in 2019"
4900:
4506:
4268:
4225:
4191:Progress in Biophysics and Molecular Biology
3961:
3908:
3902:
3757:
2985:
2907:
2864:
2487:
2485:
2408:
2406:
2404:
1935:
1933:
1413:"Shuffled domains in extracellular proteins"
5306:
5219:PIR-International Protein Sequence Database
4692:
4459:
4457:
4306:
3751:
3657:
3606:
3498:
3200:
2942:
2813:
2559:
2510:
2441:
1987:
1985:
1639:
1152:
142:
6803:
6796:
6782:
6609:
6595:
6388:
6374:
6051:
6037:
5446:
4698:
4654:
4616:"Protein structural domain identification"
4463:
4401:
4184:
4178:
3786:
3702:
3279:
2774:: CS1 maint: location missing publisher (
2256:
1991:
1852:
1802:
1520:
1349:
1297:
1117:
824:: A small protein domain from fibritin in
5902:
5852:
5834:
5817:
5799:
5753:
5710:
5638:
5501:
5421:
5324:
5244:
5135:
5034:
4981:
4932:
4831:
4734:Pandurangan AP, Topf M (September 2012).
4631:
4590:
4541:
4489:
4437:
4427:
4397:
4395:
4251:
4202:
4161:
4135:
4112:
4060:
4050:
4001:
3944:
3934:
3885:
3810:
3734:
3709:George RA, Lin K, Heringa J (July 2005).
3677:
3640:
3540:
3530:
3481:
3409:"Are there pathways for protein folding?"
3406:
3383:
3357:
3273:
3244:
3148:
3138:
3013:
2683:
2673:
2542:
2482:
2465:
2401:
2384:
2374:
2131:
2073:
2063:
1965:
1930:
1870:
1829:
1725:
1663:
1622:
1612:
1555:
1503:
1493:
1467:
1436:
1254:
1203:
1135:
5070:
4454:
4087:Sowdhamini R, Blundell TL (March 1995).
3563:
3557:
3458:"Polymer principles and protein folding"
2348:
1982:
1158:
466:
462:
321:Nature is a tinkerer and not an inventor
92:between one protein and another to make
18:
5341:
4871:
4277:
3322:
3171:
1526:
1303:
581:Advantage of domains in protein folding
373:
294:
6980:
5986:Web Archives (archived 2011-05-06)
5184:
4909:"DUFs: families in search of function"
4613:
4564:
4392:
2090:
1646:George RA, Heringa J (November 2002).
1260:
573:This has been described in terms of a
554:Protein folding - the unsolved problem
116:and by limited proteolysis studies of
6777:
6590:
6369:
6032:
5407:
5307:Hadley C, Jones DT (September 1999).
5190:Current Opinion in Structural Biology
3174:Current Opinion in Structural Biology
3113:Bork P, Doolittle RF (October 1992).
2788:
2741:
2600:
2568:Current Opinion in Structural Biology
2491:
2099:Current Opinion in Structural Biology
1079:Structural Classification of Proteins
1042:Protein structure prediction software
828:that can cause proteins to trimerize.
244:
4363:
4226:Tsai CJ, Nussinov R (January 1997).
3837:. Freeman, New York. Second edition.
3455:
2791:"wwPDB: Worldwide Protein Data Bank"
1410:
1118:Xu D, Nussinov R (1 February 1998).
891:with high affinity. Specificity for
538:Domains are autonomous folding units
6058:
5835:Yang AS, Honig B (September 1995).
5800:Yang AS, Honig B (September 1995).
5461:10.1146/annurev.bi.59.070190.003215
4516:Siddiqui AS, Barton GJ (May 1995).
3799:The Journal of Biological Chemistry
3793:Teale JM, Benjamin DC (July 1977).
2742:Bruce, Alberts (18 November 2014).
1853:Copley RR, Bork P (November 2000).
1120:"Favorable domain size in proteins"
975:due to an increasing number of new
649:One of the first algorithms used a
13:
5261:
4402:Go N, Taketomi H (February 1978).
3607:White SH, Jacobs RE (April 1990).
2132:Ghélis C, Yon JM (July 1979). "".
835:(IgSF). They contain about 70-110
725:
556: : Since the seminal work of
306:
76:, are stabilized by metal ions or
56:that is self-stabilizing and that
14:
7014:
5921:
5054:Introduction to protein structure
4464:Holm L, Sander C (January 1997).
3909:Baron R, Vellore NA (July 2012).
1181:10.1038/scientificamerican1166-78
285:
2746:(Sixth ed.). New York, NY.
989:
401:
26:, a protein with three domains (
6637:Post-translational modification
6421:Structure determination methods
5670:10.1093/bioinformatics/17.2.200
4949:
4865:
4856:
4769:
4727:
4683:
4648:
4607:
4558:
4357:
4219:
4018:
3827:
3600:
3449:
3351:
3316:
3165:
3106:
3081:
3038:
2782:
2735:
2700:
2594:
2467:10.1093/bioinformatics/16.7.613
2342:
2307:
2213:
2152:
2125:
1887:
1846:
1750:
1705:
1680:
1580:
598:Domains and protein flexibility
316:Domains as evolutionary modules
6005:NCBI Conserved Domain Database
1461:
1404:
1111:
863:Phosphotyrosine-binding domain
1:
5552:10.1016/S0022-2836(05)80134-2
5449:Annual Review of Biochemistry
5326:10.1016/S0969-2126(99)80177-4
5227:10.1016/S0076-6879(96)66005-4
5202:10.1016/S0959-440X(97)80002-4
5085:10.1016/S0065-3233(00)54006-6
5073:Advances in Protein Chemistry
5001:
4886:10.1016/S1044-5323(03)00047-2
4833:10.1093/bioinformatics/btp512
4778:Journal of Structural Biology
4755:10.1093/bioinformatics/bts446
4136:Swindells MB (January 1995).
3812:10.1016/S0021-9258(17)40192-X
3633:10.1016/S0006-3495(90)82611-4
3358:Haynie DT, Xue B (May 2015).
3186:10.1016/S0959-440X(98)80068-7
2744:Molecular biology of the cell
2580:10.1016/S0959-440X(97)80060-7
2169:10.1016/s0065-3233(01)55002-0
2111:10.1016/S0959-440X(96)80088-1
1831:10.1016/S0969-2126(97)00260-8
1368:10.1016/S0065-3233(08)60520-3
1356:Advances in Protein Chemistry
1137:10.1016/S1359-0278(98)00004-2
1100:
1023:: database of protein domains
747:): found in many DNA-binding
743:Basic leucine zipper domain (
714:A general method to identify
705:secondary structural elements
622:Database of Molecular Motions
189:(string of amino acids) of a
99:
6616:
5841:Journal of Molecular Biology
5806:Journal of Molecular Biology
5785:10.1016/0022-2836(89)90084-3
5773:Journal of Molecular Biology
5588:10.1016/0076-6879(85)15030-5
5540:Journal of Molecular Biology
5410:Journal of Molecular Biology
5393:10.1016/0022-2836(91)90388-M
5381:Journal of Molecular Biology
5170:10.1016/0022-2836(92)90634-V
5158:Journal of Molecular Biology
5052:Tooze J, Brändén CI (1999).
4378:10.1016/0022-2836(79)90363-2
4366:Journal of Molecular Biology
4292:10.1016/0022-2836(78)90043-8
4280:Journal of Molecular Biology
4204:10.1016/0079-6107(83)90003-2
3772:10.1016/0006-291X(81)91296-1
3721:(Web Server issue): W160-3.
3666:Journal of Molecular Biology
3259:10.1016/0022-2836(79)90308-5
3247:Journal of Molecular Biology
3209:Journal of Molecular Biology
3024:10.1126/science.278.5338.609
2916:Journal of Molecular Biology
2873:Journal of Molecular Biology
2721:10.1016/0167-7799(94)90078-7
2222:Journal of Molecular Biology
1859:Journal of Molecular Biology
1714:Journal of Molecular Biology
1614:10.1371/journal.pone.0012736
1438:10.1016/0014-5793(91)80937-X
1326:10.1126/science.180.4088.830
1283:10.1126/science.180.4087.713
1037:Protein structure prediction
516:protein tyrosine phosphatase
7:
6017:Functional domain databases
5927:Structural domain databases
5574:Janin J, Chothia C (1985).
2161:Evolutionary Protein Design
1468:Wetlaufer DB (March 1973).
1010:Cofactor transferase family
982:
956:Domains of unknown function
612:domains, induce long-range
62:three-dimensional structure
10:
7019:
6678:Protein structural domains
6397:Protein tertiary structure
5959: (archived 2006-09-11)
4185:Janin J, Wodak SJ (1983).
2349:Savageau MA (March 1986).
968:domain of unknown function
962:Domain of unknown function
959:
885:Pleckstrin homology domain
833:immunoglobulin superfamily
814:and in the muscle protein
644:
601:
546:
542:
178:
175:Units of protein structure
147:An appropriate example is
6965:Nucleic acid double helix
6917:
6864:
6811:
6691:
6665:
6624:
6568:
6537:
6496:
6465:
6429:
6403:
6066:
5969:Sequence domain databases
5056:. New York: Garland Pub.
4925:10.1107/S1744309110001685
4790:10.1016/j.jsb.2011.10.011
3994:10.1016/j.bpj.2010.09.058
3878:10.1016/j.bpj.2009.03.051
3833:Creighton, T. E. (1983).
3566:Nature Structural Biology
3337:10.1093/protein/7.12.1407
2928:10.1016/j.jmb.2005.02.007
2603:"Evolution and tinkering"
1665:10.1093/protein/15.11.871
881:responses of human cells.
481:domain-domain interaction
428:
4633:10.1093/protein/12.3.203
4614:Taylor WR (March 1999).
709:cryo electron microscopy
449:homologous recombination
220:supersecondary structure
143:Example: Pyruvate kinase
5011:"The Protein Data Bank"
4565:Zehfus MH (June 1997).
4052:10.1073/pnas.0503388102
3936:10.1073/pnas.1207892109
3532:10.1073/pnas.89.18.8721
3140:10.1073/pnas.89.19.8990
2709:Trends in Biotechnology
2675:10.1186/1471-2164-9-452
2427:10.1093/protein/8.6.513
2328:10.1093/protein/6.3.233
737:Drosophila melanogaster
655:hierarchical clustering
618:protein domain dynamics
218:and are referred to as
6866:Nucleic acid structure
6805:Biomolecular structure
5883:Nucleic Acids Research
5854:10.1006/jmbi.1995.0503
5819:10.1006/jmbi.1995.0502
5734:Nucleic Acids Research
5691:Nucleic Acids Research
5619:Nucleic Acids Research
5482:Nucleic Acids Research
5432:10.1006/jmbi.1999.3006
5116:Nucleic Acids Research
5015:Nucleic Acids Research
4962:Nucleic Acids Research
4874:Seminars in Immunology
4583:10.1002/pro.5560060609
4534:10.1002/pro.5560040507
4470:Nucleic Acids Research
4244:10.1002/pro.5560060104
4154:10.1002/pro.5560040113
4105:10.1002/pro.5560040317
3715:Nucleic Acids Research
3688:10.1006/jmbi.2001.5387
3436:10.1051/jcp/1968650044
3294:10.1002/bies.950180308
3221:10.1006/jmbi.1996.0050
2963:10.1002/bies.950150303
2885:10.1006/jmbi.2001.4776
2627:10.1126/science.860134
2535:10.1002/pro.5560041202
2376:10.1073/pnas.83.5.1198
2234:10.1006/jmbi.1998.2374
2065:10.1073/pnas.47.9.1309
2006:10.1002/prot.340190309
1958:10.1002/pro.5560070202
1908:10.1002/prot.340050208
1872:10.1006/jmbi.2000.4152
1736:10.1006/jmbi.1999.2661
1350:Richardson JS (1981).
1052:Protein tandem repeats
887:(PH): PH domains bind
476:
471:Insertions of similar
131:function and evolution
37:
7003:Protein superfamilies
6741:Photoreceptor protein
6473:Immunoglobulin domain
4429:10.1073/pnas.75.2.559
3456:Dill KA (June 1999).
2601:Jacob F (June 1977).
1692:proteinstructures.com
1495:10.1073/pnas.70.3.697
945:transcription factors
916:Src homology 2 domain
777:Death effector domain
547:Further information:
470:
463:Types of organization
299:Many proteins have a
22:
6632:Protein biosynthesis
5895:10.1093/nar/30.1.268
5703:10.1093/nar/27.1.284
5631:10.1093/nar/28.1.231
5494:10.1093/nar/28.1.260
5027:10.1093/nar/28.1.235
4482:10.1093/nar/25.1.231
3445:on 2 September 2009.
3407:Levinthal C (1968).
1411:Bork P (July 1991).
1124:Folding & Design
922:, which is itself a
374:Multidomain proteins
301:quaternary structure
295:Quaternary structure
239:Structural alignment
6935:Protein engineering
6509:Leucine-rich repeat
5984:Library of Congress
5746:10.1093/nar/29.1.22
5276:1981Natur.291...90G
5128:10.1093/nar/29.1.55
4713:10.1021/bi00367a062
4669:10.1021/bi00526a005
4620:Protein Engineering
4420:1978PNAS...75..559G
4327:1974Natur.250..194R
4043:2005PNAS..10217646B
3986:2010BpJ....99.3473F
3974:Biophysical Journal
3927:2012PNAS..10912509B
3870:2009BpJ....96.4993P
3858:Biophysical Journal
3625:1990BpJ....57..911W
3613:Biophysical Journal
3523:1992PNAS...89.8721L
3474:10.1110/ps.8.6.1166
3428:1968JCP....65...44L
3325:Protein Engineering
3131:1992PNAS...89.8990B
3006:1997Sci...278..609H
2834:1994Natur.372..631O
2619:1977Sci...196.1161J
2415:Protein Engineering
2367:1986PNAS...83.1198S
2316:Protein Engineering
2277:1976Natur.261..552L
2056:1961PNAS...47.1309A
1772:1975Natur.255..609B
1652:Protein Engineering
1605:2010PLoSO...512736B
1548:1992Natur.357..543C
1486:1973PNAS...70..697W
1429:1991FEBSL.286...47B
1392:on 10 February 2019
1318:1973Sci...180..830E
1275:1973Sci...180..713P
1224:1968Natur.218..929D
1173:1966SciAm.215e..78P
1161:Scientific American
1047:Protein superfamily
458:during replication.
355:Molecular evolution
226:. For example, the
201:secondary structure
104:The concept of the
90:genetic engineering
66:Molecular evolution
4974:10.1093/nar/gky995
4919:(Pt 10): 1148–52.
3727:10.1093/nar/gki381
3578:10.1038/nsb0197-10
3089:"SMART: Main page"
1074:Structural biology
1069:Short linear motif
972:Pfam database
941:DNA-binding domain
847:and other charged
651:Cα-Cα distance map
477:
413:(scrollable image)
393:GAR transformylase
345:fibronectin type 3
253:tertiary structure
245:Tertiary structure
38:
6988:Protein structure
6973:
6972:
6813:Protein structure
6771:
6770:
6673:Protein structure
6647:Protein targeting
6584:
6583:
6529:Trefoil knot fold
6411:Structural domain
6363:
6362:
5963:PFAM clan browser
5597:978-0-12-182015-2
5569:on 26 April 2012.
5236:978-0-12-182167-8
5094:978-0-12-034254-9
5063:978-0-8153-2305-1
4968:(D1): D427–D432.
3864:(12): 4993–5002.
3059:10.1002/dvg.20351
2503:978-0-7167-7027-5
1062:Protein subfamily
1032:Protein structure
889:phosphoinositides
809:signaling protein
805:structural domain
732:Armadillo repeats
716:dynamical domains
685:domain database.
626:neutron spin echo
566:Levinthal paradox
360:Protein Data Bank
216:protein structure
187:primary structure
181:Protein structure
128:compact structure
122:protein structure
94:chimeric proteins
78:disulfide bridges
54:polypeptide chain
48:is a region of a
42:molecular biology
7010:
6998:Protein families
6960:Structural motif
6798:
6791:
6784:
6775:
6774:
6751:Phycobiliprotein
6709:Globular protein
6704:Membrane protein
6699:List of proteins
6611:
6604:
6597:
6588:
6587:
6569:Irregular folds:
6524:Thioredoxin fold
6447:Homeodomain fold
6390:
6383:
6376:
6367:
6366:
6053:
6046:
6039:
6030:
6029:
5916:
5906:
5877:(January 2002).
5866:
5856:
5831:
5821:
5796:
5767:
5757:
5724:
5714:
5681:
5652:
5642:
5609:
5570:
5568:
5562:. Archived from
5537:
5515:
5505:
5472:
5443:
5425:
5404:
5375:
5338:
5328:
5303:
5284:10.1038/291090a0
5258:
5248:
5213:
5181:
5149:
5139:
5106:
5067:
5048:
5038:
4996:
4995:
4985:
4953:
4947:
4946:
4936:
4904:
4898:
4897:
4869:
4863:
4860:
4854:
4853:
4835:
4811:
4802:
4801:
4773:
4767:
4766:
4740:
4731:
4725:
4724:
4696:
4690:
4687:
4681:
4680:
4652:
4646:
4645:
4635:
4611:
4605:
4604:
4594:
4562:
4556:
4555:
4545:
4513:
4504:
4503:
4493:
4461:
4452:
4451:
4441:
4431:
4399:
4390:
4389:
4361:
4355:
4354:
4335:10.1038/250194a0
4310:
4304:
4303:
4275:
4266:
4265:
4255:
4223:
4217:
4216:
4206:
4182:
4176:
4175:
4165:
4133:
4127:
4126:
4116:
4084:
4075:
4074:
4064:
4054:
4037:(49): 17646–51.
4022:
4016:
4015:
4005:
3965:
3959:
3958:
3948:
3938:
3921:(31): 12509–14.
3906:
3900:
3899:
3889:
3849:
3838:
3831:
3825:
3824:
3814:
3790:
3784:
3783:
3755:
3749:
3748:
3738:
3706:
3700:
3699:
3681:
3661:
3655:
3654:
3644:
3604:
3598:
3597:
3561:
3555:
3554:
3544:
3534:
3502:
3496:
3495:
3485:
3453:
3447:
3446:
3444:
3438:. Archived from
3413:
3404:
3398:
3397:
3387:
3376:10.1002/pro.2664
3355:
3349:
3348:
3320:
3314:
3313:
3277:
3271:
3270:
3242:
3233:
3232:
3204:
3198:
3197:
3169:
3163:
3162:
3152:
3142:
3110:
3104:
3103:
3101:
3099:
3085:
3079:
3078:
3042:
3036:
3035:
3017:
3000:(5338): 609–14.
2989:
2983:
2982:
2946:
2940:
2939:
2911:
2905:
2904:
2868:
2862:
2861:
2842:10.1038/372631a0
2817:
2811:
2810:
2808:
2806:
2797:. Archived from
2786:
2780:
2779:
2773:
2765:
2739:
2733:
2732:
2704:
2698:
2697:
2687:
2677:
2653:
2647:
2646:
2613:(4295): 1161–6.
2598:
2592:
2591:
2563:
2557:
2556:
2546:
2514:
2508:
2507:
2489:
2480:
2479:
2469:
2445:
2439:
2438:
2410:
2399:
2398:
2388:
2378:
2346:
2340:
2339:
2311:
2305:
2304:
2285:10.1038/261552a0
2260:
2254:
2253:
2217:
2211:
2210:
2204:
2200:
2198:
2190:
2156:
2150:
2149:
2129:
2123:
2122:
2094:
2088:
2087:
2077:
2067:
2035:
2026:
2025:
1989:
1980:
1979:
1969:
1937:
1928:
1927:
1891:
1885:
1884:
1874:
1850:
1844:
1843:
1833:
1809:
1800:
1799:
1780:10.1038/255609a0
1766:(5510): 609–14.
1754:
1748:
1747:
1729:
1709:
1703:
1702:
1700:
1698:
1684:
1678:
1677:
1667:
1643:
1637:
1636:
1626:
1616:
1584:
1578:
1577:
1559:
1557:10.1038/357543a0
1524:
1518:
1517:
1507:
1497:
1465:
1459:
1458:
1440:
1408:
1402:
1401:
1399:
1397:
1388:. Archived from
1347:
1338:
1337:
1312:(4088): 830–40.
1301:
1295:
1294:
1258:
1252:
1251:
1232:10.1038/218929a0
1218:(5145): 929–32.
1207:
1201:
1200:
1156:
1150:
1149:
1139:
1115:
1095:Structural motif
999:
994:
993:
977:genome sequences
826:T4 bacteriophage
801:structural motif
798:helix-turn-helix
653:together with a
504:ABC transporters
405:
278:domain database.
153:protein families
35:
7018:
7017:
7013:
7012:
7011:
7009:
7008:
7007:
6993:Protein domains
6978:
6977:
6974:
6969:
6913:
6860:
6807:
6802:
6772:
6767:
6731:Fibrous protein
6687:
6661:
6657:Protein methods
6642:Protein folding
6620:
6615:
6585:
6580:
6564:
6550:Ferredoxin fold
6533:
6514:Flavodoxin fold
6492:
6461:
6425:
6416:Protein folding
6399:
6394:
6364:
6359:
6062:
6060:Protein domains
6057:
6019:
5971:
5957:Wayback Machine
5929:
5924:
5919:
5598:
5566:
5535:
5319:(9): 1099–112.
5237:
5095:
5064:
5004:
4999:
4954:
4950:
4905:
4901:
4870:
4866:
4861:
4857:
4812:
4805:
4774:
4770:
4738:
4732:
4728:
4707:(19): 5759–65.
4697:
4693:
4688:
4684:
4663:(23): 6544–52.
4653:
4649:
4612:
4608:
4571:Protein Science
4563:
4559:
4522:Protein Science
4514:
4507:
4462:
4455:
4400:
4393:
4362:
4358:
4311:
4307:
4276:
4269:
4232:Protein Science
4224:
4220:
4183:
4179:
4142:Protein Science
4134:
4130:
4093:Protein Science
4085:
4078:
4023:
4019:
3980:(10): 3473–82.
3966:
3962:
3907:
3903:
3850:
3841:
3832:
3828:
3791:
3787:
3756:
3752:
3707:
3703:
3679:10.1.1.329.2921
3662:
3658:
3605:
3601:
3562:
3558:
3503:
3499:
3462:Protein Science
3454:
3450:
3442:
3411:
3405:
3401:
3364:Protein Science
3356:
3352:
3331:(12): 1407–10.
3321:
3317:
3278:
3274:
3243:
3236:
3205:
3201:
3170:
3166:
3111:
3107:
3097:
3095:
3087:
3086:
3082:
3043:
3039:
3015:10.1.1.562.2262
2990:
2986:
2947:
2943:
2912:
2908:
2869:
2865:
2828:(6507): 631–4.
2818:
2814:
2804:
2802:
2801:on 7 April 2015
2787:
2783:
2767:
2766:
2754:
2740:
2736:
2705:
2701:
2654:
2650:
2599:
2595:
2564:
2560:
2529:(12): 2455–68.
2523:Protein Science
2515:
2511:
2504:
2494:Protein Folding
2490:
2483:
2446:
2442:
2411:
2402:
2361:(5): 1198–202.
2347:
2343:
2312:
2308:
2271:(5561): 552–8.
2261:
2257:
2218:
2214:
2202:
2201:
2192:
2191:
2179:
2157:
2153:
2130:
2126:
2095:
2091:
2036:
2029:
1990:
1983:
1946:Protein Science
1938:
1931:
1892:
1888:
1851:
1847:
1824:(8): 1093–108.
1810:
1803:
1755:
1751:
1727:10.1.1.217.9806
1710:
1706:
1696:
1694:
1686:
1685:
1681:
1644:
1640:
1585:
1581:
1542:(6379): 543–4.
1525:
1521:
1466:
1462:
1409:
1405:
1395:
1393:
1378:
1348:
1341:
1302:
1298:
1269:(4087): 713–6.
1259:
1255:
1208:
1204:
1157:
1153:
1116:
1112:
1103:
995:
988:
985:
964:
958:
924:tyrosine kinase
909:PtdIns(3,4,5)P3
728:
726:Example domains
660:Cα-Cα distances
647:
634:
610:flexible linker
606:
600:
583:
551:
549:Protein folding
545:
540:
493:serine protease
465:
431:
426:
425:
424:
411:
406:
376:
318:
309:
307:Domain swapping
297:
288:
247:
183:
177:
149:pyruvate kinase
145:
118:immunoglobulins
102:
27:
24:Pyruvate kinase
17:
12:
11:
5:
7016:
7006:
7005:
7000:
6995:
6990:
6971:
6970:
6968:
6967:
6962:
6957:
6952:
6947:
6942:
6937:
6932:
6930:Protein domain
6927:
6921:
6919:
6915:
6914:
6912:
6911:
6909:Thermodynamics
6906:
6901:
6896:
6891:
6886:
6881:
6876:
6870:
6868:
6862:
6861:
6859:
6858:
6856:Thermodynamics
6853:
6848:
6843:
6838:
6833:
6828:
6823:
6817:
6815:
6809:
6808:
6801:
6800:
6793:
6786:
6778:
6769:
6768:
6766:
6765:
6764:
6763:
6758:
6753:
6743:
6738:
6733:
6728:
6727:
6726:
6721:
6716:
6706:
6701:
6695:
6693:
6689:
6688:
6686:
6685:
6680:
6675:
6669:
6667:
6663:
6662:
6660:
6659:
6654:
6649:
6644:
6639:
6634:
6628:
6626:
6622:
6621:
6614:
6613:
6606:
6599:
6591:
6582:
6581:
6579:
6578:
6572:
6570:
6566:
6565:
6563:
6562:
6557:
6555:Ribonuclease A
6552:
6547:
6541:
6539:
6535:
6534:
6532:
6531:
6526:
6521:
6516:
6511:
6506:
6500:
6498:
6494:
6493:
6491:
6490:
6485:
6483:Beta-propeller
6480:
6475:
6469:
6467:
6463:
6462:
6460:
6459:
6454:
6452:Alpha solenoid
6449:
6444:
6439:
6433:
6431:
6427:
6426:
6424:
6423:
6418:
6413:
6407:
6405:
6401:
6400:
6393:
6392:
6385:
6378:
6370:
6361:
6360:
6358:
6357:
6352:
6347:
6342:
6337:
6332:
6327:
6322:
6317:
6312:
6307:
6302:
6301:
6300:
6290:
6285:
6280:
6275:
6270:
6265:
6260:
6255:
6250:
6245:
6240:
6235:
6230:
6225:
6220:
6215:
6214:
6213:
6208:
6203:
6198:
6188:
6183:
6178:
6173:
6168:
6163:
6158:
6153:
6148:
6143:
6138:
6133:
6128:
6123:
6118:
6113:
6108:
6103:
6098:
6093:
6088:
6083:
6078:
6073:
6067:
6064:
6063:
6056:
6055:
6048:
6041:
6033:
6027:
6026:
6018:
6015:
6014:
6013:
6007:
6002:
5997:
5992:
5987:
5977:
5970:
5967:
5966:
5965:
5960:
5950:
5945:
5940:
5935:
5928:
5925:
5923:
5922:External links
5920:
5918:
5917:
5867:
5832:
5797:
5768:
5725:
5682:
5658:Bioinformatics
5653:
5610:
5596:
5571:
5531:(April 1995).
5516:
5473:
5444:
5423:10.1.1.332.955
5405:
5376:
5339:
5304:
5270:(5810): 90–2.
5259:
5235:
5214:
5182:
5150:
5107:
5093:
5068:
5062:
5049:
5005:
5003:
5000:
4998:
4997:
4948:
4899:
4864:
4855:
4826:(20): 2743–4.
4820:Bioinformatics
4803:
4768:
4749:(18): 2391–3.
4743:Bioinformatics
4726:
4691:
4682:
4647:
4606:
4557:
4505:
4453:
4391:
4356:
4321:(463): 194–9.
4305:
4267:
4218:
4177:
4128:
4076:
4017:
3960:
3901:
3839:
3826:
3805:(13): 4521–6.
3785:
3750:
3701:
3656:
3599:
3556:
3517:(18): 8721–5.
3497:
3468:(6): 1166–80.
3448:
3399:
3350:
3315:
3272:
3234:
3199:
3164:
3125:(19): 8990–4.
3105:
3080:
3053:(12): 744–56.
3037:
2984:
2941:
2906:
2863:
2812:
2781:
2752:
2734:
2699:
2648:
2593:
2558:
2509:
2502:
2481:
2454:Bioinformatics
2440:
2400:
2341:
2306:
2255:
2212:
2203:|journal=
2177:
2151:
2124:
2089:
2050:(9): 1309–14.
2027:
1981:
1929:
1886:
1845:
1801:
1749:
1704:
1679:
1638:
1579:
1519:
1480:(3): 697–701.
1460:
1423:(1–2): 47–54.
1403:
1376:
1339:
1296:
1253:
1202:
1151:
1109:
1108:
1107:
1102:
1099:
1098:
1097:
1092:
1090:Sequence motif
1087:
1082:
1076:
1071:
1066:
1065:
1064:
1059:
1057:Protein family
1054:
1049:
1044:
1039:
1034:
1024:
1018:
1012:
1007:
1005:Binding domain
1001:
1000:
997:Biology portal
984:
981:
960:Main article:
957:
954:
953:
952:
935:
913:
882:
860:
829:
819:
803:found in each
791:
774:
764:
741:
727:
724:
711:density maps.
672:The method of
646:
643:
633:
630:
628:spectroscopy.
602:Main article:
599:
596:
582:
579:
575:folding funnel
544:
541:
539:
536:
464:
461:
460:
459:
456:DNA polymerase
452:
446:
443:
430:
427:
408:
407:
400:
399:
398:
389:AIR synthetase
385:GAR synthetase
375:
372:
341:immunoglobulin
317:
314:
308:
305:
296:
293:
287:
286:Limits on size
284:
283:
282:
279:
272:
268:
257:protein family
246:
243:
179:Main article:
176:
173:
144:
141:
136:
135:
132:
129:
101:
98:
82:EF hand domain
46:protein domain
15:
9:
6:
4:
3:
2:
7015:
7004:
7001:
6999:
6996:
6994:
6991:
6989:
6986:
6985:
6983:
6976:
6966:
6963:
6961:
6958:
6956:
6953:
6951:
6948:
6946:
6943:
6941:
6938:
6936:
6933:
6931:
6928:
6926:
6923:
6922:
6920:
6916:
6910:
6907:
6905:
6902:
6900:
6897:
6895:
6894:Determination
6892:
6890:
6887:
6885:
6882:
6880:
6877:
6875:
6872:
6871:
6869:
6867:
6863:
6857:
6854:
6852:
6849:
6847:
6844:
6842:
6841:Determination
6839:
6837:
6834:
6832:
6829:
6827:
6824:
6822:
6819:
6818:
6816:
6814:
6810:
6806:
6799:
6794:
6792:
6787:
6785:
6780:
6779:
6776:
6762:
6759:
6757:
6754:
6752:
6749:
6748:
6747:
6744:
6742:
6739:
6737:
6736:Chromoprotein
6734:
6732:
6729:
6725:
6722:
6720:
6717:
6715:
6712:
6711:
6710:
6707:
6705:
6702:
6700:
6697:
6696:
6694:
6690:
6684:
6681:
6679:
6676:
6674:
6671:
6670:
6668:
6664:
6658:
6655:
6653:
6650:
6648:
6645:
6643:
6640:
6638:
6635:
6633:
6630:
6629:
6627:
6623:
6619:
6612:
6607:
6605:
6600:
6598:
6593:
6592:
6589:
6577:
6574:
6573:
6571:
6567:
6561:
6560:SH2-like fold
6558:
6556:
6553:
6551:
6548:
6546:
6543:
6542:
6540:
6536:
6530:
6527:
6525:
6522:
6520:
6519:Rossmann fold
6517:
6515:
6512:
6510:
6507:
6505:
6502:
6501:
6499:
6495:
6489:
6486:
6484:
6481:
6479:
6476:
6474:
6471:
6470:
6468:
6464:
6458:
6455:
6453:
6450:
6448:
6445:
6443:
6440:
6438:
6435:
6434:
6432:
6428:
6422:
6419:
6417:
6414:
6412:
6409:
6408:
6406:
6402:
6398:
6391:
6386:
6384:
6379:
6377:
6372:
6371:
6368:
6356:
6353:
6351:
6348:
6346:
6343:
6341:
6338:
6336:
6333:
6331:
6328:
6326:
6323:
6321:
6318:
6316:
6313:
6311:
6308:
6306:
6303:
6299:
6296:
6295:
6294:
6291:
6289:
6286:
6284:
6281:
6279:
6276:
6274:
6271:
6269:
6266:
6264:
6261:
6259:
6256:
6254:
6251:
6249:
6246:
6244:
6241:
6239:
6236:
6234:
6231:
6229:
6226:
6224:
6221:
6219:
6216:
6212:
6209:
6207:
6204:
6202:
6199:
6197:
6194:
6193:
6192:
6189:
6187:
6184:
6182:
6179:
6177:
6174:
6172:
6169:
6167:
6164:
6162:
6159:
6157:
6154:
6152:
6149:
6147:
6144:
6142:
6139:
6137:
6134:
6132:
6129:
6127:
6124:
6122:
6119:
6117:
6114:
6112:
6109:
6107:
6104:
6102:
6099:
6097:
6094:
6092:
6089:
6087:
6084:
6082:
6079:
6077:
6074:
6072:
6069:
6068:
6065:
6061:
6054:
6049:
6047:
6042:
6040:
6035:
6034:
6031:
6024:
6021:
6020:
6011:
6008:
6006:
6003:
6001:
5998:
5996:
5993:
5991:
5988:
5985:
5981:
5978:
5976:
5973:
5972:
5964:
5961:
5958:
5954:
5951:
5949:
5946:
5944:
5941:
5939:
5936:
5934:
5931:
5930:
5914:
5910:
5905:
5900:
5896:
5892:
5889:(1): 268–72.
5888:
5884:
5880:
5876:
5872:
5868:
5864:
5860:
5855:
5850:
5847:(3): 366–76.
5846:
5842:
5838:
5833:
5829:
5825:
5820:
5815:
5812:(3): 351–65.
5811:
5807:
5803:
5798:
5794:
5790:
5786:
5782:
5778:
5774:
5769:
5765:
5761:
5756:
5751:
5747:
5743:
5739:
5735:
5731:
5726:
5722:
5718:
5713:
5708:
5704:
5700:
5696:
5692:
5688:
5683:
5679:
5675:
5671:
5667:
5663:
5659:
5654:
5650:
5646:
5641:
5636:
5632:
5628:
5624:
5620:
5616:
5611:
5607:
5603:
5599:
5593:
5589:
5585:
5581:
5577:
5572:
5565:
5561:
5557:
5553:
5549:
5546:(4): 536–40.
5545:
5541:
5534:
5530:
5526:
5522:
5517:
5513:
5509:
5504:
5499:
5495:
5491:
5487:
5483:
5479:
5474:
5470:
5466:
5462:
5458:
5455:(1): 631–60.
5454:
5450:
5445:
5441:
5437:
5433:
5429:
5424:
5419:
5416:(2): 283–93.
5415:
5411:
5406:
5402:
5398:
5394:
5390:
5387:(1): 151–71.
5386:
5382:
5377:
5373:
5369:
5365:
5361:
5357:
5353:
5350:(4): 425–35.
5349:
5345:
5340:
5336:
5332:
5327:
5322:
5318:
5314:
5310:
5305:
5301:
5297:
5293:
5289:
5285:
5281:
5277:
5273:
5269:
5265:
5260:
5256:
5252:
5247:
5242:
5238:
5232:
5228:
5224:
5220:
5215:
5211:
5207:
5203:
5199:
5195:
5191:
5187:
5183:
5179:
5175:
5171:
5167:
5164:(3): 819–35.
5163:
5159:
5155:
5151:
5147:
5143:
5138:
5133:
5129:
5125:
5121:
5117:
5113:
5108:
5104:
5100:
5096:
5090:
5086:
5082:
5078:
5074:
5069:
5065:
5059:
5055:
5050:
5046:
5042:
5037:
5032:
5028:
5024:
5021:(1): 235–42.
5020:
5016:
5012:
5007:
5006:
4993:
4989:
4984:
4979:
4975:
4971:
4967:
4963:
4959:
4952:
4944:
4940:
4935:
4930:
4926:
4922:
4918:
4914:
4910:
4903:
4895:
4891:
4887:
4883:
4880:(4): 215–23.
4879:
4875:
4868:
4859:
4851:
4847:
4843:
4839:
4834:
4829:
4825:
4821:
4817:
4810:
4808:
4799:
4795:
4791:
4787:
4784:(2): 520–31.
4783:
4779:
4772:
4764:
4760:
4756:
4752:
4748:
4744:
4737:
4730:
4722:
4718:
4714:
4710:
4706:
4702:
4695:
4686:
4678:
4674:
4670:
4666:
4662:
4658:
4651:
4643:
4639:
4634:
4629:
4626:(3): 203–16.
4625:
4621:
4617:
4610:
4602:
4598:
4593:
4588:
4584:
4580:
4577:(6): 1210–9.
4576:
4572:
4568:
4561:
4553:
4549:
4544:
4539:
4535:
4531:
4528:(5): 872–84.
4527:
4523:
4519:
4512:
4510:
4501:
4497:
4492:
4487:
4483:
4479:
4475:
4471:
4467:
4460:
4458:
4449:
4445:
4440:
4435:
4430:
4425:
4421:
4417:
4414:(2): 559–63.
4413:
4409:
4405:
4398:
4396:
4387:
4383:
4379:
4375:
4372:(3): 447–70.
4371:
4367:
4360:
4352:
4348:
4344:
4340:
4336:
4332:
4328:
4324:
4320:
4316:
4309:
4301:
4297:
4293:
4289:
4286:(3): 315–32.
4285:
4281:
4274:
4272:
4263:
4259:
4254:
4249:
4245:
4241:
4237:
4233:
4229:
4222:
4214:
4210:
4205:
4200:
4196:
4192:
4188:
4181:
4173:
4169:
4164:
4159:
4155:
4151:
4148:(1): 103–12.
4147:
4143:
4139:
4132:
4124:
4120:
4115:
4110:
4106:
4102:
4099:(3): 506–20.
4098:
4094:
4090:
4083:
4081:
4072:
4068:
4063:
4058:
4053:
4048:
4044:
4040:
4036:
4032:
4028:
4021:
4013:
4009:
4004:
3999:
3995:
3991:
3987:
3983:
3979:
3975:
3971:
3964:
3956:
3952:
3947:
3942:
3937:
3932:
3928:
3924:
3920:
3916:
3912:
3905:
3897:
3893:
3888:
3883:
3879:
3875:
3871:
3867:
3863:
3859:
3855:
3848:
3846:
3844:
3836:
3830:
3822:
3818:
3813:
3808:
3804:
3800:
3796:
3789:
3781:
3777:
3773:
3769:
3765:
3761:
3754:
3746:
3742:
3737:
3732:
3728:
3724:
3720:
3716:
3712:
3705:
3697:
3693:
3689:
3685:
3680:
3675:
3672:(3): 839–51.
3671:
3667:
3660:
3652:
3648:
3643:
3638:
3634:
3630:
3626:
3622:
3619:(4): 911–21.
3618:
3614:
3610:
3603:
3595:
3591:
3587:
3583:
3579:
3575:
3571:
3567:
3560:
3552:
3548:
3543:
3538:
3533:
3528:
3524:
3520:
3516:
3512:
3508:
3501:
3493:
3489:
3484:
3479:
3475:
3471:
3467:
3463:
3459:
3452:
3441:
3437:
3433:
3429:
3425:
3421:
3417:
3410:
3403:
3395:
3391:
3386:
3381:
3377:
3373:
3370:(5): 874–82.
3369:
3365:
3361:
3354:
3346:
3342:
3338:
3334:
3330:
3326:
3319:
3311:
3307:
3303:
3299:
3295:
3291:
3288:(3): 207–19.
3287:
3283:
3276:
3268:
3264:
3260:
3256:
3252:
3248:
3241:
3239:
3230:
3226:
3222:
3218:
3215:(4): 604–16.
3214:
3210:
3203:
3195:
3191:
3187:
3183:
3180:(3): 338–45.
3179:
3175:
3168:
3160:
3156:
3151:
3146:
3141:
3136:
3132:
3128:
3124:
3120:
3116:
3109:
3094:
3093:smart.embl.de
3090:
3084:
3076:
3072:
3068:
3064:
3060:
3056:
3052:
3048:
3041:
3033:
3029:
3025:
3021:
3016:
3011:
3007:
3003:
2999:
2995:
2988:
2980:
2976:
2972:
2968:
2964:
2960:
2957:(3): 157–64.
2956:
2952:
2945:
2937:
2933:
2929:
2925:
2922:(1): 231–43.
2921:
2917:
2910:
2902:
2898:
2894:
2890:
2886:
2882:
2879:(2): 311–25.
2878:
2874:
2867:
2859:
2855:
2851:
2847:
2843:
2839:
2835:
2831:
2827:
2823:
2816:
2800:
2796:
2792:
2785:
2777:
2771:
2763:
2759:
2755:
2753:9780815344322
2749:
2745:
2738:
2730:
2726:
2722:
2718:
2715:(5): 168–72.
2714:
2710:
2703:
2695:
2691:
2686:
2681:
2676:
2671:
2667:
2663:
2659:
2652:
2644:
2640:
2636:
2632:
2628:
2624:
2620:
2616:
2612:
2608:
2604:
2597:
2589:
2585:
2581:
2577:
2574:(3): 416–21.
2573:
2569:
2562:
2554:
2550:
2545:
2540:
2536:
2532:
2528:
2524:
2520:
2513:
2505:
2499:
2495:
2488:
2486:
2477:
2473:
2468:
2463:
2459:
2455:
2451:
2444:
2436:
2432:
2428:
2424:
2421:(6): 513–25.
2420:
2416:
2409:
2407:
2405:
2396:
2392:
2387:
2382:
2377:
2372:
2368:
2364:
2360:
2356:
2352:
2345:
2337:
2333:
2329:
2325:
2322:(3): 233–45.
2321:
2317:
2310:
2302:
2298:
2294:
2290:
2286:
2282:
2278:
2274:
2270:
2266:
2259:
2251:
2247:
2243:
2239:
2235:
2231:
2228:(4): 1371–5.
2227:
2223:
2216:
2208:
2196:
2188:
2184:
2180:
2178:9780120342556
2174:
2170:
2166:
2162:
2155:
2147:
2143:
2139:
2135:
2128:
2120:
2116:
2112:
2108:
2104:
2100:
2093:
2085:
2081:
2076:
2071:
2066:
2061:
2057:
2053:
2049:
2045:
2041:
2034:
2032:
2023:
2019:
2015:
2011:
2007:
2003:
2000:(3): 256–68.
1999:
1995:
1988:
1986:
1977:
1973:
1968:
1963:
1959:
1955:
1952:(2): 233–42.
1951:
1947:
1943:
1936:
1934:
1925:
1921:
1917:
1913:
1909:
1905:
1902:(2): 139–48.
1901:
1897:
1890:
1882:
1878:
1873:
1868:
1865:(4): 627–41.
1864:
1860:
1856:
1849:
1841:
1837:
1832:
1827:
1823:
1819:
1815:
1808:
1806:
1797:
1793:
1789:
1785:
1781:
1777:
1773:
1769:
1765:
1761:
1753:
1745:
1741:
1737:
1733:
1728:
1723:
1720:(1): 147–64.
1719:
1715:
1708:
1693:
1689:
1683:
1675:
1671:
1666:
1661:
1658:(11): 871–9.
1657:
1653:
1649:
1642:
1634:
1630:
1625:
1620:
1615:
1610:
1606:
1602:
1599:(9): e12736.
1598:
1594:
1590:
1583:
1575:
1571:
1567:
1563:
1558:
1553:
1549:
1545:
1541:
1537:
1533:
1530:(June 1992).
1529:
1523:
1515:
1511:
1506:
1501:
1496:
1491:
1487:
1483:
1479:
1475:
1471:
1464:
1456:
1452:
1448:
1444:
1439:
1434:
1430:
1426:
1422:
1418:
1414:
1407:
1391:
1387:
1383:
1379:
1377:9780120342341
1373:
1369:
1365:
1361:
1357:
1353:
1346:
1344:
1335:
1331:
1327:
1323:
1319:
1315:
1311:
1307:
1300:
1292:
1288:
1284:
1280:
1276:
1272:
1268:
1264:
1257:
1249:
1245:
1241:
1237:
1233:
1229:
1225:
1221:
1217:
1213:
1206:
1198:
1194:
1190:
1186:
1182:
1178:
1174:
1170:
1166:
1162:
1155:
1147:
1143:
1138:
1133:
1129:
1125:
1121:
1114:
1110:
1105:
1104:
1096:
1093:
1091:
1088:
1086:
1083:
1080:
1077:
1075:
1072:
1070:
1067:
1063:
1060:
1058:
1055:
1053:
1050:
1048:
1045:
1043:
1040:
1038:
1035:
1033:
1030:
1029:
1028:
1025:
1022:
1019:
1016:
1013:
1011:
1008:
1006:
1003:
1002:
998:
992:
987:
980:
978:
973:
969:
963:
950:
946:
942:
939:
936:
933:
929:
925:
921:
917:
914:
910:
906:
905:PtdIns(4,5)P2
902:
901:PtdIns(3,4)P2
898:
894:
890:
886:
883:
880:
876:
872:
868:
864:
861:
858:
857:immune system
854:
853:cell adhesion
850:
846:
842:
838:
834:
830:
827:
823:
822:Foldon domain
820:
817:
813:
810:
806:
802:
799:
795:
792:
789:
785:
782:
778:
775:
772:
768:
765:
762:
758:
754:
750:
746:
742:
739:
738:
733:
730:
729:
723:
721:
717:
712:
710:
706:
702:
697:
694:
690:
686:
684:
678:
675:
670:
668:
663:
661:
656:
652:
642:
638:
629:
627:
623:
619:
615:
611:
605:
595:
591:
587:
578:
576:
570:
567:
562:
559:
555:
550:
535:
533:
529:
525:
521:
517:
511:
507:
505:
501:
496:
494:
491:
486:
482:
474:
469:
457:
453:
450:
447:
444:
441:
440:
439:
436:
422:
421:Kelch domains
418:
414:
410:
404:
397:
394:
390:
386:
380:
371:
367:
365:
361:
356:
352:
350:
346:
342:
338:
334:
330:
326:
322:
313:
304:
302:
292:
280:
277:
273:
269:
266:
265:
264:
262:
258:
254:
249:
242:
240:
236:
232:
229:
225:
221:
217:
212:
210:
206:
202:
197:
192:
188:
182:
172:
168:
165:
161:
156:
154:
150:
140:
133:
130:
127:
126:
125:
123:
119:
115:
111:
107:
97:
95:
91:
87:
83:
79:
75:
71:
67:
63:
59:
55:
51:
47:
43:
34:
30:
25:
21:
6975:
6945:Nucleic acid
6929:
6677:
6466:All-β folds:
6437:Helix bundle
6430:All-α folds:
6410:
6059:
5886:
5882:
5844:
5840:
5809:
5805:
5776:
5772:
5737:
5733:
5697:(1): 284–5.
5694:
5690:
5664:(2): 200–1.
5661:
5657:
5625:(1): 231–4.
5622:
5618:
5579:
5564:the original
5543:
5539:
5488:(1): 260–2.
5485:
5481:
5452:
5448:
5413:
5409:
5384:
5380:
5347:
5343:
5316:
5312:
5267:
5263:
5218:
5193:
5189:
5161:
5157:
5119:
5115:
5076:
5072:
5053:
5018:
5014:
4965:
4961:
4951:
4916:
4912:
4902:
4877:
4873:
4867:
4858:
4823:
4819:
4781:
4777:
4771:
4746:
4742:
4729:
4704:
4701:Biochemistry
4700:
4694:
4689:Rashin, 1985
4685:
4660:
4657:Biochemistry
4656:
4650:
4623:
4619:
4609:
4574:
4570:
4560:
4525:
4521:
4476:(1): 231–4.
4473:
4469:
4411:
4407:
4369:
4365:
4359:
4318:
4314:
4308:
4283:
4279:
4238:(1): 24–42.
4235:
4231:
4221:
4197:(1): 21–78.
4194:
4190:
4180:
4145:
4141:
4131:
4096:
4092:
4034:
4030:
4020:
3977:
3973:
3963:
3918:
3914:
3904:
3861:
3857:
3834:
3829:
3802:
3798:
3788:
3766:(2): 563–9.
3763:
3759:
3753:
3718:
3714:
3704:
3669:
3665:
3659:
3616:
3612:
3602:
3569:
3565:
3559:
3514:
3510:
3500:
3465:
3461:
3451:
3440:the original
3419:
3415:
3402:
3367:
3363:
3353:
3328:
3324:
3318:
3285:
3281:
3275:
3253:(1): 49–79.
3250:
3246:
3212:
3208:
3202:
3177:
3173:
3167:
3122:
3118:
3108:
3096:. Retrieved
3092:
3083:
3050:
3046:
3040:
2997:
2993:
2987:
2954:
2950:
2944:
2919:
2915:
2909:
2876:
2872:
2866:
2825:
2821:
2815:
2803:. Retrieved
2799:the original
2794:
2784:
2743:
2737:
2712:
2708:
2702:
2665:
2662:BMC Genomics
2661:
2651:
2610:
2606:
2596:
2571:
2567:
2561:
2526:
2522:
2512:
2493:
2460:(7): 613–8.
2457:
2453:
2443:
2418:
2414:
2358:
2354:
2344:
2319:
2315:
2309:
2268:
2264:
2258:
2225:
2221:
2215:
2160:
2154:
2140:(2): 197–9.
2137:
2133:
2127:
2102:
2098:
2092:
2047:
2043:
1997:
1993:
1949:
1945:
1899:
1895:
1889:
1862:
1858:
1848:
1821:
1817:
1763:
1759:
1752:
1717:
1713:
1707:
1695:. Retrieved
1691:
1682:
1655:
1651:
1641:
1596:
1592:
1582:
1539:
1535:
1522:
1477:
1473:
1463:
1420:
1417:FEBS Letters
1416:
1406:
1394:. Retrieved
1390:the original
1359:
1355:
1309:
1305:
1299:
1266:
1262:
1256:
1215:
1211:
1205:
1167:(5): 78–90.
1164:
1160:
1154:
1127:
1123:
1113:
967:
965:
927:
753:dimerization
735:
715:
713:
698:
691:
687:
679:
671:
664:
648:
639:
635:
607:
592:
588:
584:
571:
563:
553:
552:
512:
508:
497:
490:chymotrypsin
478:
454:slippage of
432:
412:
381:
377:
368:
353:
320:
319:
310:
298:
289:
250:
248:
237:
233:
213:
184:
169:
157:
146:
137:
105:
103:
74:zinc fingers
45:
39:
6756:Phytochrome
6746:Biliprotein
6478:Beta barrel
6442:Globin fold
6355:zinc finger
6010:SUPERFAMILY
5779:(1): 1–22.
5740:(1): 22–8.
5519:Murzin AG,
5122:(1): 55–7.
3572:(1): 10–9.
3416:J Chim Phys
2795:www.pdb.org
2789:wwPDB.org.
2105:(1): 3–10.
1362:: 167–339.
1130:(1): 11–7.
938:Zinc finger
849:amino acids
841:beta sheets
837:amino acids
745:bZIP domain
699:The method
693:RigidFinder
667:dendrograms
70:amino acids
6982:Categories
6940:Proteasome
6899:Prediction
6889:Quaternary
6846:Prediction
6836:Quaternary
6683:Proteasome
6666:Structures
6538:α+β folds:
6504:TIM barrel
6497:α/β folds:
6488:Beta helix
6457:Death fold
5521:Brenner SE
5196:(1): 3–9.
5079:: 159–83.
5002:Key papers
1697:14 October
1101:References
932:SH3 domain
897:PtdIns(4)P
893:PtdIns(3)P
873:bind to a
816:troponin-C
812:calmodulin
749:eukaryotic
164:TIM barrel
100:Background
86:calmodulin
6879:Secondary
6826:Secondary
6761:Lipocalin
6625:Processes
6576:Conotoxin
6545:DNA clamp
6243:EcoEI_R_C
5875:Chothia C
5529:Chothia C
5525:Hubbard T
5418:CiteSeerX
5313:Structure
5186:Fersht AR
3674:CiteSeerX
3422:: 44–45.
3282:BioEssays
3098:1 January
3010:CiteSeerX
2951:BioEssays
2770:cite book
2762:887605755
2205:ignored (
2195:cite book
1818:Structure
1722:CiteSeerX
1528:Chothia C
1396:3 January
949:promoters
845:cysteines
788:apoptosis
784:proteases
614:allostery
520:C2 domain
473:PH domain
435:evolution
228:β-hairpin
205:α-helices
36:).
6918:See also
6884:Tertiary
6831:Tertiary
6714:Globulin
6652:Proteome
6618:Proteins
5975:InterPro
5913:11752312
5764:11125040
5678:11238081
5649:10592234
5512:10592241
5440:10550209
5372:29808315
5364:10450084
5344:Proteins
5335:10508779
5154:Dyson HJ
5146:11125048
5103:10829228
5045:10592235
4992:30357350
4943:20944204
4894:14690046
4850:28106759
4842:19696046
4798:22079400
4763:22796953
4642:10235621
4071:16306270
4012:21081097
3955:22802671
3896:19527659
3745:15980446
3696:11866536
3594:11557990
3492:10386867
3394:25694109
3310:46012215
3075:20878849
3067:18064672
2979:24897614
2936:15808866
2901:11894663
2893:11428892
2694:18828911
2643:29756896
2476:11038331
2187:11050932
2084:13683522
1994:Proteins
1924:15340449
1896:Proteins
1881:11054297
1744:10329133
1674:12538906
1633:20856875
1593:PLOS ONE
1455:22126481
1197:39959172
983:See also
928:See also
920:oncogene
786:trigger
771:adhesion
767:Cadherin
757:arginine
558:Anfinsen
522:pair in
500:kinesins
347:and the
329:Bacteria
209:β-sheets
196:residues
134:folding.
110:lysozyme
6925:Protein
6874:Primary
6821:Primary
6724:Albumin
6719:Edestin
6404:General
6273:Kringle
6166:CGI-121
6136:BTB/POZ
5990:PROSITE
5982:at the
5955:at the
5871:Gough J
5863:7563057
5828:7563056
5793:2769748
5721:9847202
5606:4079796
5560:7723011
5469:2197986
5401:2067014
5300:4313732
5292:7231530
5272:Bibcode
5255:8743676
5210:9032066
5178:1507228
4983:6324024
4934:2954198
4721:3778881
4677:7306523
4601:9194181
4592:2143719
4552:7663343
4543:2143117
4500:9016542
4416:Bibcode
4351:4273028
4343:4368490
4323:Bibcode
4262:9007974
4253:2143523
4213:6353481
4172:7773168
4163:2142966
4123:7795532
4114:2143076
4062:1345721
4039:Bibcode
4003:2980739
3982:Bibcode
3946:3411975
3923:Bibcode
3887:2712024
3866:Bibcode
3780:7306096
3736:1160142
3651:2188687
3642:1280792
3621:Bibcode
3586:8989315
3551:1528885
3519:Bibcode
3483:2144345
3424:Bibcode
3385:4420535
3345:7716150
3302:8867735
3229:8568900
3194:9666330
3159:1409594
3127:Bibcode
3047:Genesis
3032:9381171
3002:Bibcode
2994:Science
2971:8098212
2858:4330359
2850:7990952
2830:Bibcode
2805:25 July
2729:7764899
2685:2576256
2668:: 452.
2615:Bibcode
2607:Science
2588:9204285
2553:8580836
2544:2143041
2435:8532675
2395:3513170
2363:Bibcode
2336:8506258
2301:4154884
2273:Bibcode
2250:8702994
2242:9917381
2119:8696970
2052:Bibcode
2014:7937738
1976:9521098
1967:2143930
1916:2664768
1840:9309224
1796:4195346
1788:1134550
1768:Bibcode
1624:2939071
1601:Bibcode
1574:4355476
1566:1608464
1544:Bibcode
1514:4351801
1482:Bibcode
1447:1864378
1425:Bibcode
1386:7020376
1334:4540988
1314:Bibcode
1306:Science
1291:4122075
1271:Bibcode
1263:Science
1248:4169127
1240:5681232
1220:Bibcode
1189:5978599
1169:Bibcode
1146:9502316
1027:Protein
879:insulin
807:of the
794:EF hand
781:Caspase
701:RIBFIND
645:Methods
543:Folding
532:auxilin
349:kringle
333:Eukarya
325:Archaea
261:classes
191:protein
50:protein
6904:Design
6851:Design
5995:ProDom
5911:
5901:
5861:
5826:
5791:
5762:
5752:
5719:
5712:148157
5709:
5676:
5647:
5640:102444
5637:
5604:
5594:
5558:
5510:
5503:102474
5500:
5467:
5438:
5420:
5399:
5370:
5362:
5333:
5298:
5290:
5264:Nature
5253:
5246:145575
5243:
5233:
5208:
5176:
5144:
5134:
5101:
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