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Membrane protein

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Although membrane proteins play an important role in all organisms, their purification has historically, and continues to be, a huge challenge for protein scientists. In 2008, 150 unique structures of membrane proteins were available, and by 2019 only 50 human membrane proteins had had their
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Membrane proteins are common, and medically important—about a third of all human proteins are membrane proteins, and these are targets for more than half of all drugs. Nonetheless, compared to other classes of proteins, determining membrane
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are transmembrane proteins that span across the membrane only once. Transmembrane helices from these proteins have significantly different amino acid distributions to transmembrane helices from polytopic
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Hochuli E, Bannwarth W, Döbeli H, Gentz R, Stüber D (November 1988). "Genetic Approach to Facilitate Purification of Recombinant Proteins with a Novel Metal Chelate Adsorbent".
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are thought to be membrane proteins, 600 of which have been experimentally verified to be membrane resident. In humans, current thinking suggests that fully 30% of the
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Daley DO, Rapp M, Granseth E, Melén K, Drew D, von Heijne G (May 2005). "Global topology analysis of the Escherichia coli inner membrane proteome".
365:, and other non-covalent interactions. Peripheral proteins dissociate following treatment with a polar reagent, such as a solution with an elevated 663:"Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin" 57:. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a 2026: 1839: 1776:- Database of 3D structures of integral membrane proteins and hydrophobic peptides with an emphasis on crystallization conditions 81:
remains a challenge in large part due to the difficulty in establishing experimental conditions that can preserve the correct (
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Cook BL, Steuerwald D, Kaiser L, Graveland-Bikker J, Vanberghem M, Berke AP, Herlihy K, Pick H, Vogel H, Zhang S (July 2009).
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is a commonly used tag for membrane protein purification, and the alternative rho1D4 tag has also been successfully used.
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are integral membrane proteins that are attached to only one side of the membrane and do not span the whole way across.
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Sun C, Benlekbir S, Venkatakrishnan P, Wang Y, Hong S, Hosler J, Tajkhorshid E, Rubinstein JL, Gennis RB (May 2018).
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are permanently attached to the membrane. Such proteins can be separated from the biological membranes only using
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Schematic representation of the different types of interaction between monotopic membrane proteins and the
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are transmembrane proteins that span across the membrane more than once. These proteins may have different
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structures elucidated. In contrast, approximately 25% of all proteins are membrane proteins. Their
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Overington JP, Al-Lazikani B, Hopkins AL (December 2006). "How many drug targets are there?".
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ones, taking great care to maintain secondary structure while revising overall charge.
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Membrane proteins perform a variety of functions vital to the survival of organisms:
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allow cells to identify each other and interact. For example, proteins involved in
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Integral and peripheral proteins may be post-translationally modified, with added
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Lin Y, Fuerst O, Granell M, Leblanc G, LĂłrenz-FonfrĂ­a V, PadrĂłs E (August 2013).
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surfaces make structural and especially functional characterization difficult.
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encode for membrane proteins. For instance, about 1000 of the ~4200 proteins of
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Proceedings of the National Academy of Sciences of the United States of America
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parallel to the membrane plane (in-plane membrane helix) 2. interaction by a
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The localization of proteins in membranes can be predicted reliably using
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Locatelli-Hoops SC, Gorshkova I, Gawrisch K, Yeliseev AA (October 2013).
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Baker JA, Wong WC, Eisenhaber B, Warwicker J, Eisenhaber F (July 2017).
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is one of the best solutions for purification of membrane proteins. The
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agents. They can be classified according to their relationship with the
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Andreeva A, Howorth D, Chothia C, Kulesha E, Murzin AG (January 2014).
529: 517: 373: 324: 315: 166: 163: 30: 1733:, a comprehensive classification of transmembrane transporter proteins 311: 194: 186: 1991: 418: 414: 217: 142: 105: 39: 1543: 780: 631: 2174: 2124: 1944: 1882: 421:, are sometimes considered a separate category. These proteins are 1954: 1949: 1848: 661:
Almén MS, Nordström KJ, Fredriksson R, Schiöth HB (August 2009).
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Proteins that are part of, or interact with, biological membranes
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Krogh A, Larsson B, von Heijne G, Sonnhammer EL (January 2001).
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across the membrane. They can be categorized according to the
1789:- A curated list of selected transmembrane proteins from the 1501:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
1016:"SCOP2 prototype: a new approach to protein structure mining" 1013: 860:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
587: 1750: 898: 615: 1817: 1457: 462: 243:. These proteins have one of two structural architectures: 1766: 1294:
Carpenter EP, Beis K, Cameron AD, Iwata S (October 2008).
1798:- a database of membrane protein structures simulated by 1293: 119: 65:) or associate with one or the other side of a membrane ( 1709: 854:
Selkrig J, Leyton DL, Webb CT, Lithgow T (August 2014).
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Experts for Membrane Protein Research and Purification
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Orientations of Proteins in Membranes (OPM) database
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Cell and Molecular Biology: Concepts and Experiments
510: 2034: 73:are transiently associated with the cell membrane. 720:Biochimica et Biophysica Acta (BBA) - Biomembranes 461:, are common. It is estimated that 20–30% of all 1409:"Membrane proteins: always an insoluble problem?" 2187: 1246:"Elucidating the Structure of Membrane Proteins" 1710:Membrane Protein Structural Dynamics Consortium 1067:"Dissecting the Structure of Membrane Proteins" 294: 162:of protein sequences, i.e. the localization of 1607: 765:(December 2006). "Membrane-protein topology". 611: 609: 590:(TransMembrane Protein Helix-Packing Database) 2020: 1833: 1720: 1644: 172: 1757:approximately arranged in the lipid bilayer. 1243: 1072:Genetic Engineering & Biotechnology News 357:or to integral proteins by a combination of 249:proteins, which are present in all types of 1751:Protein Data Bank of Transmembrane Proteins 1389:on 2020-08-04 – via Semantic Scholar. 950: 809: 606: 318:loop 3. interaction by a covalently bound 199:The membrane is represented in light-brown. 2027: 2013: 1840: 1826: 847: 761: 104:proteins relay signals between the cell's 89:in isolation from its native environment. 1680: 1627: 1581: 1571: 1520: 1434: 1319: 1263: 1064: 1041: 990: 926: 916: 871: 731: 690: 680: 1406: 1244:Martin, Joseph; Sawyer, Abigail (2019). 524:can be used to render membrane proteins 298: 176: 29: 803: 353:are temporarily attached either to the 61:and can either penetrate the membrane ( 14: 2188: 768:Nature Reviews. Molecular Cell Biology 2008: 1821: 1300:Current Opinion in Structural Biology 1239: 1237: 1235: 1233: 1231: 1229: 1168: 391: 744:– via Elsevier Science Direct. 53:that are part of, or interact with, 1731:Transporter Classification database 417:, and certain proteins involved in 124:Transporter Classification database 24: 1663:10.1016/b978-0-12-417027-8.00003-9 1601: 1226: 1058: 259:proteins, which are found only in 133:may have many activities, such as 25: 2207: 1698: 511:Purification of membrane proteins 1703: 1414:Biochemical Society Transactions 1392: 1279: 1218: 1160: 1105:, Sonnhammer EL (January 2001). 942: 747: 449:Membrane proteins, like soluble 1868:Post-translational modification 1608:Johnson JE, Cornell RB (1999). 1537: 1488: 1451: 1400: 1336: 1287: 1091: 563:Inner nuclear membrane proteins 1645:Alenghat FJ, Golan DE (2013). 1258:(4). Future Science: 167–170. 1065:Liszewski K (1 October 2015). 1007: 892: 755: 707: 654: 619:Nature Reviews. Drug Discovery 34:Membrane protein complexes of 13: 1: 1747:arranged in the lipid bilayer 600: 482: 444: 369:or high salt concentrations. 1847: 1814:from several model organisms 1745:peripheral membrane proteins 1513:10.1016/j.bbapap.2013.06.003 1352:Journal of Molecular Biology 1115:Journal of Molecular Biology 873:10.1016/j.bbamcr.2013.10.009 733:10.1016/j.bbamem.2013.03.003 578:List of MeSH codes (D12.776) 425:but can undergo significant 351:Peripheral membrane proteins 295:Peripheral membrane proteins 185:: 1. a single transmembrane 181:Schematic representation of 71:Peripheral membrane proteins 7: 2105:Peripheral membrane protein 1810:provides information about 1651:Current Topics in Membranes 545: 479:encodes membrane proteins. 346:Peripheral membrane protein 288:Integral monotopic proteins 237:Integral polytopic proteins 92: 87:conformation of the protein 10: 2212: 2096:Integral membrane proteins 1909:Protein structural domains 1721:Membrane protein databases 1615:Molecular Membrane Biology 1153:on 2020-08-04 – via 1028:(Database issue): D310-4. 491:of over 50% of all modern 487:Membrane proteins are the 395: 343: 214:Integral membrane proteins 202: 173:Integral membrane proteins 2117: 2081: 2043: 1922: 1896: 1855: 1407:Rawlings AE (June 2016). 1312:10.1016/j.sbi.2008.07.001 983:10.1038/s41586-018-0061-y 918:10.1186/s12915-017-0404-4 267:, and outer membranes of 205:Integral membrane protein 191:bitopic membrane protein 2140:Lipid raft/microdomains 1629:10.1080/096876899294544 1573:10.1073/pnas.0811089106 1197:10.1126/science.1109730 583:Receptor (biochemistry) 536:Affinity chromatography 437:or reversibly with the 328:) 4. electrostatic or 307:: 1. interaction by an 160:hydrophobicity analyses 149:Cell adhesion molecules 2145:Membrane contact sites 2109:Lipid-anchored protein 2091:Membrane glycoproteins 1755:transmembrane proteins 1364:10.1006/jmbi.2000.4315 1128:10.1006/jmbi.2000.4315 1021:Nucleic Acids Research 682:10.1186/1741-7007-7-50 594:Transmembrane proteins 427:conformational changes 407:antibacterial peptides 341: 332:with membrane lipids ( 265:Gram-negative bacteria 241:transmembrane topology 200: 183:transmembrane proteins 43: 2100:transmembrane protein 1972:Photoreceptor protein 1265:10.2144/btn-2019-0030 884:– via Elsevier 302: 209:Transmembrane protein 180: 33: 2125:Caveolae/Coated pits 1863:Protein biosynthesis 1474:10.1038/nbt1188-1321 1461:Nature Biotechnology 1085:10.1089/gen.35.17.02 1079:(17): 1, 14, 16–17. 810:Gerald Karp (2009). 431:oligomeric complexes 251:biological membranes 55:biological membranes 1808:Membranome database 1739:- 3D structures of 1564:2009PNAS..10611925C 1427:10.1042/BST20160025 1189:2005Sci...308.1321D 1034:10.1093/nar/gkt1242 975:2018Natur.557..123S 820:John Wiley and Sons 553:Annular lipid shell 459:disordered proteins 118:move molecules and 2150:Membrane nanotubes 2035:Structures of the 1803:molecular dynamics 1785:2013-12-25 at the 1772:2020-08-03 at the 573:Ion pump (biology) 398:Pore-forming toxin 392:Polypeptide toxins 342: 330:ionic interactions 201: 116:Transport proteins 79:protein structures 67:integral monotopic 44: 2196:Membrane proteins 2183: 2182: 2083:Membrane proteins 2002: 2001: 1904:Protein structure 1878:Protein targeting 1791:Protein Data Bank 1468:(11): 1321–1325. 969:(7703): 123–126. 829:978-0-470-48337-4 822:. pp. 128–. 540:polyhistidine-tag 451:globular proteins 222:nonpolar solvents 102:Membrane receptor 47:Membrane proteins 18:Membrane proteins 16:(Redirected from 2203: 2165:Nuclear envelope 2160:Nodes of Ranvier 2029: 2022: 2015: 2006: 2005: 1982:Phycobiliprotein 1940:Globular protein 1935:Membrane protein 1930:List of proteins 1842: 1835: 1828: 1819: 1818: 1812:bitopic proteins 1780:Mpstruc database 1694: 1684: 1641: 1631: 1596: 1595: 1585: 1575: 1558:(29): 11925–30. 1541: 1535: 1534: 1524: 1492: 1486: 1485: 1455: 1449: 1448: 1438: 1404: 1398: 1397: 1396: 1390: 1388: 1382:. Archived from 1349: 1340: 1334: 1333: 1323: 1291: 1285: 1284: 1283: 1277: 1267: 1241: 1224: 1223: 1222: 1216: 1183:(5726): 1321–3. 1172: 1166: 1165: 1164: 1158: 1155:Semantic Scholar 1152: 1146:. Archived from 1111: 1095: 1089: 1088: 1062: 1056: 1055: 1045: 1011: 1005: 1004: 994: 954: 948: 947: 946: 940: 930: 920: 896: 890: 889: 875: 851: 845: 844: 838: 836: 817: 807: 801: 800: 759: 753: 752: 751: 745: 735: 711: 705: 704: 694: 684: 658: 652: 651: 613: 455:fibrous proteins 405:toxins and many 281:Bitopic proteins 21: 2211: 2210: 2206: 2205: 2204: 2202: 2201: 2200: 2186: 2185: 2184: 2179: 2113: 2077: 2045:Membrane lipids 2039: 2033: 2003: 1998: 1962:Fibrous protein 1918: 1892: 1888:Protein methods 1873:Protein folding 1851: 1846: 1787:Wayback Machine 1774:Wayback Machine 1753:- 3D models of 1723: 1706: 1701: 1673: 1604: 1602:Further reading 1599: 1542: 1538: 1507:(10): 2045–56. 1493: 1489: 1456: 1452: 1405: 1401: 1391: 1386: 1347: 1341: 1337: 1292: 1288: 1278: 1254:(Print issue). 1242: 1227: 1217: 1173: 1169: 1159: 1150: 1109: 1096: 1092: 1063: 1059: 1012: 1008: 955: 951: 941: 897: 893: 852: 848: 834: 832: 830: 808: 804: 781:10.1038/nrm2063 760: 756: 746: 712: 708: 659: 655: 632:10.1038/nrd2199 614: 607: 603: 598: 558:Carrier protein 548: 513: 505:cystic fibrosis 493:medicinal drugs 485: 447: 400: 394: 348: 297: 261:outer membranes 224:, or sometimes 211: 203:Main articles: 198: 175: 153:immune response 95: 28: 23: 22: 15: 12: 11: 5: 2209: 2199: 2198: 2181: 2180: 2178: 2177: 2172: 2170:Phycobilisomes 2167: 2162: 2157: 2152: 2147: 2142: 2137: 2132: 2130:Cell junctions 2127: 2121: 2119: 2115: 2114: 2112: 2111: 2102: 2093: 2087: 2085: 2079: 2078: 2076: 2075: 2070: 2065: 2060: 2055: 2049: 2047: 2041: 2040: 2032: 2031: 2024: 2017: 2009: 2000: 1999: 1997: 1996: 1995: 1994: 1989: 1984: 1974: 1969: 1964: 1959: 1958: 1957: 1952: 1947: 1937: 1932: 1926: 1924: 1920: 1919: 1917: 1916: 1911: 1906: 1900: 1898: 1894: 1893: 1891: 1890: 1885: 1880: 1875: 1870: 1865: 1859: 1857: 1853: 1852: 1845: 1844: 1837: 1830: 1822: 1816: 1815: 1805: 1800:coarse-grained 1793: 1777: 1764: 1758: 1748: 1734: 1722: 1719: 1718: 1717: 1712: 1705: 1702: 1700: 1699:External links 1697: 1696: 1695: 1671: 1642: 1603: 1600: 1598: 1597: 1536: 1487: 1450: 1399: 1335: 1286: 1225: 1167: 1090: 1057: 1006: 949: 891: 886:Science Direct 866:(8): 1542–50. 846: 828: 802: 775:(12): 909–18. 754: 706: 653: 604: 602: 599: 597: 596: 591: 585: 580: 575: 570: 565: 560: 555: 549: 547: 544: 512: 509: 484: 481: 446: 443: 433:and associate 396:Main article: 393: 390: 378:diacylglycerol 344:Main article: 320:membrane lipid 296: 293: 292: 291: 285: 278: 277: 276: 254: 174: 171: 156: 155: 146: 135:oxidoreductase 127: 113: 94: 91: 36:photosynthesis 26: 9: 6: 4: 3: 2: 2208: 2197: 2194: 2193: 2191: 2176: 2173: 2171: 2168: 2166: 2163: 2161: 2158: 2156: 2155:Myelin sheath 2153: 2151: 2148: 2146: 2143: 2141: 2138: 2136: 2133: 2131: 2128: 2126: 2123: 2122: 2120: 2116: 2110: 2106: 2103: 2101: 2097: 2094: 2092: 2089: 2088: 2086: 2084: 2080: 2074: 2071: 2069: 2068:Sphingolipids 2066: 2064: 2061: 2059: 2058:Phospholipids 2056: 2054: 2053:Lipid bilayer 2051: 2050: 2048: 2046: 2042: 2038: 2037:cell membrane 2030: 2025: 2023: 2018: 2016: 2011: 2010: 2007: 1993: 1990: 1988: 1985: 1983: 1980: 1979: 1978: 1975: 1973: 1970: 1968: 1967:Chromoprotein 1965: 1963: 1960: 1956: 1953: 1951: 1948: 1946: 1943: 1942: 1941: 1938: 1936: 1933: 1931: 1928: 1927: 1925: 1921: 1915: 1912: 1910: 1907: 1905: 1902: 1901: 1899: 1895: 1889: 1886: 1884: 1881: 1879: 1876: 1874: 1871: 1869: 1866: 1864: 1861: 1860: 1858: 1854: 1850: 1843: 1838: 1836: 1831: 1829: 1824: 1823: 1820: 1813: 1809: 1806: 1804: 1801: 1797: 1794: 1792: 1788: 1784: 1781: 1778: 1775: 1771: 1768: 1765: 1762: 1759: 1756: 1752: 1749: 1746: 1742: 1738: 1735: 1732: 1728: 1725: 1724: 1716: 1713: 1711: 1708: 1707: 1704:Organizations 1692: 1688: 1683: 1678: 1674: 1672:9780124170278 1668: 1664: 1660: 1656: 1652: 1648: 1643: 1639: 1635: 1630: 1625: 1622:(3): 217–35. 1621: 1617: 1616: 1611: 1606: 1605: 1593: 1589: 1584: 1579: 1574: 1569: 1565: 1561: 1557: 1553: 1552: 1547: 1540: 1532: 1528: 1523: 1518: 1514: 1510: 1506: 1502: 1498: 1491: 1483: 1479: 1475: 1471: 1467: 1463: 1462: 1454: 1446: 1442: 1437: 1432: 1428: 1424: 1420: 1416: 1415: 1410: 1403: 1395: 1385: 1381: 1377: 1373: 1369: 1365: 1361: 1358:(3): 567–80. 1357: 1353: 1346: 1339: 1331: 1327: 1322: 1317: 1313: 1309: 1305: 1301: 1297: 1290: 1282: 1275: 1271: 1266: 1261: 1257: 1253: 1252: 1251:BioTechniques 1248:. Tech News. 1247: 1240: 1238: 1236: 1234: 1232: 1230: 1221: 1214: 1210: 1206: 1202: 1198: 1194: 1190: 1186: 1182: 1178: 1171: 1163: 1156: 1149: 1145: 1141: 1137: 1133: 1129: 1125: 1122:(3): 567–80. 1121: 1117: 1116: 1108: 1104: 1101:, Larsson B, 1100: 1094: 1086: 1082: 1078: 1074: 1073: 1068: 1061: 1053: 1049: 1044: 1039: 1035: 1031: 1027: 1023: 1022: 1017: 1010: 1002: 998: 993: 988: 984: 980: 976: 972: 968: 964: 960: 953: 945: 938: 934: 929: 924: 919: 914: 910: 906: 902: 895: 887: 883: 879: 874: 869: 865: 861: 857: 850: 842: 831: 825: 821: 816: 815: 806: 798: 794: 790: 786: 782: 778: 774: 770: 769: 764: 758: 750: 743: 739: 734: 729: 726:(8): 1690–9. 725: 721: 717: 710: 702: 698: 693: 688: 683: 678: 674: 670: 669: 664: 657: 649: 645: 641: 637: 633: 629: 626:(12): 993–6. 625: 621: 620: 612: 610: 605: 595: 592: 589: 586: 584: 581: 579: 576: 574: 571: 569: 566: 564: 561: 559: 556: 554: 551: 550: 543: 541: 537: 533: 531: 527: 526:water-soluble 523: 519: 508: 506: 502: 498: 497:heart disease 494: 490: 480: 478: 474: 473: 468: 464: 460: 456: 452: 442: 440: 439:lipid bilayer 436: 432: 428: 424: 423:water-soluble 420: 416: 412: 408: 404: 399: 389: 387: 383: 379: 375: 370: 368: 364: 363:electrostatic 360: 356: 355:lipid bilayer 352: 347: 339: 335: 331: 327: 326: 321: 317: 313: 310: 306: 305:cell membrane 301: 289: 286: 282: 279: 274: 270: 266: 262: 258: 255: 252: 248: 245: 244: 242: 238: 235: 234: 233: 231: 227: 223: 219: 215: 210: 206: 196: 192: 188: 184: 179: 170: 168: 165: 161: 154: 150: 147: 144: 140: 136: 132: 128: 125: 121: 117: 114: 112:environments. 111: 107: 103: 100: 99: 98: 90: 88: 84: 80: 74: 72: 68: 64: 63:transmembrane 60: 59:cell membrane 56: 52: 48: 41: 37: 32: 19: 2082: 2063:Lipoproteins 1934: 1767:Membrane PDB 1654: 1650: 1619: 1613: 1555: 1549: 1539: 1504: 1500: 1490: 1465: 1459: 1453: 1421:(3): 790–5. 1418: 1412: 1402: 1384:the original 1355: 1351: 1338: 1306:(5): 581–6. 1303: 1299: 1289: 1255: 1249: 1180: 1176: 1170: 1148:the original 1119: 1113: 1103:von Heijne G 1093: 1076: 1070: 1060: 1025: 1019: 1009: 966: 962: 952: 908: 904: 894: 863: 859: 849: 841:Google Books 839:– via 833:. Retrieved 813: 805: 772: 766: 763:von Heijne G 757: 723: 719: 709: 672: 666: 656: 623: 617: 534: 514: 486: 470: 448: 435:irreversibly 401: 371: 349: 333: 323: 273:chloroplasts 269:mitochondria 247:Helix bundle 212: 157: 96: 75: 46: 45: 1987:Phytochrome 1977:Biliprotein 1761:TransportDB 905:BMC Biology 835:13 November 668:BMC Biology 622:(Opinion). 568:Ion channel 530:hydrophilic 518:hydrophobic 501:Alzheimer's 403:Polypeptide 384:chains, or 359:hydrophobic 338:calcium ion 316:hydrophobic 309:amphipathic 257:Beta barrel 169:sequences. 164:hydrophobic 139:transferase 49:are common 2135:Glycocalyx 1914:Proteasome 1897:Structures 1657:: 89–120. 1179:(Report). 601:References 522:Detergents 483:In disease 445:In genomes 415:hemolysins 409:, such as 374:fatty acid 336:through a 325:lipidation 226:denaturing 218:detergents 167:amino acid 2175:Porosomes 1992:Lipocalin 1856:Processes 1796:MemProtMD 1075:(paper). 911:(1): 66. 419:apoptosis 284:proteins. 143:hydrolase 129:Membrane 40:thylakoid 2190:Category 1945:Globulin 1883:Proteome 1849:Proteins 1783:Archived 1770:Archived 1741:integral 1691:24210428 1638:10503244 1592:19581598 1531:23777860 1445:27284043 1380:15769874 1372:11152613 1330:18674618 1274:30987442 1205:15919996 1144:15769874 1136:11152613 1052:24293656 1001:29695868 937:28738801 882:24135059 797:22218266 789:17139331 742:23500619 701:19678920 648:11979420 640:17139284 546:See also 465:in most 411:colicins 197:protein 110:external 106:internal 93:Function 51:proteins 42:membrane 2073:Sterols 1955:Albumin 1950:Edestin 1682:4193470 1583:2715541 1560:Bibcode 1522:3779079 1482:9518666 1436:4900757 1321:2580798 1213:6942424 1185:Bibcode 1177:Science 1099:Krogh A 1043:3964979 992:6004266 971:Bibcode 928:5525207 692:2739160 489:targets 472:E. coli 467:genomes 429:, form 312:α-helix 230:bilayer 195:β-sheet 187:α-helix 131:enzymes 38:in the 1689:  1679:  1669:  1636:  1590:  1580:  1529:  1519:  1480:  1443:  1433:  1378:  1370:  1328:  1318:  1272:  1211:  1203:  1142:  1134:  1050:  1040:  999:  989:  963:Nature 935:  925:  880:  826:  795:  787:  740:  699:  689:  675:: 50. 646:  638:  477:genome 457:, and 382:prenyl 83:native 2118:Other 1923:Types 1478:S2CID 1387:(PDF) 1376:S2CID 1348:(PDF) 1209:S2CID 1151:(PDF) 1140:S2CID 1110:(PDF) 793:S2CID 644:S2CID 588:TMPad 463:genes 1743:and 1727:TCDB 1687:PMID 1667:ISBN 1634:PMID 1588:PMID 1527:PMID 1505:1834 1441:PMID 1368:PMID 1326:PMID 1270:PMID 1201:PMID 1132:PMID 1048:PMID 997:PMID 933:PMID 878:PMID 864:1843 837:2010 824:ISBN 785:PMID 738:PMID 724:1828 697:PMID 636:PMID 503:and 334:e.g. 271:and 207:and 120:ions 108:and 1677:PMC 1659:doi 1624:doi 1578:PMC 1568:doi 1556:106 1517:PMC 1509:doi 1470:doi 1431:PMC 1423:doi 1360:doi 1356:305 1316:PMC 1308:doi 1260:doi 1193:doi 1181:308 1124:doi 1120:305 1081:doi 1038:PMC 1030:doi 987:PMC 979:doi 967:557 923:PMC 913:doi 868:doi 777:doi 728:doi 687:PMC 677:doi 628:doi 413:or 386:GPI 380:or 263:of 141:or 69:). 2192:: 1729:- 1685:. 1675:. 1665:. 1655:72 1653:. 1649:. 1632:. 1620:16 1618:. 1612:. 1586:. 1576:. 1566:. 1554:. 1548:. 1525:. 1515:. 1503:. 1499:. 1476:. 1464:. 1439:. 1429:. 1419:44 1417:. 1411:. 1374:. 1366:. 1354:. 1350:. 1324:. 1314:. 1304:18 1302:. 1298:. 1268:. 1256:66 1228:^ 1207:. 1199:. 1191:. 1138:. 1130:. 1118:. 1112:. 1077:35 1069:. 1046:. 1036:. 1026:42 1024:. 1018:. 995:. 985:. 977:. 965:. 961:. 931:. 921:. 909:15 907:. 903:. 876:. 862:. 858:. 818:. 791:. 783:. 771:. 736:. 722:. 718:. 695:. 685:. 671:. 665:. 642:. 634:. 608:^ 507:. 499:, 453:, 441:. 376:, 367:pH 361:, 232:: 220:, 137:, 85:) 2107:/ 2098:/ 2028:e 2021:t 2014:v 1841:e 1834:t 1827:v 1693:. 1661:: 1640:. 1626:: 1594:. 1570:: 1562:: 1533:. 1511:: 1484:. 1472:: 1466:6 1447:. 1425:: 1362:: 1332:. 1310:: 1276:. 1262:: 1215:. 1195:: 1187:: 1157:. 1126:: 1087:. 1083:: 1054:. 1032:: 1003:. 981:: 973:: 939:. 915:: 888:. 870:: 843:. 799:. 779:: 773:7 730:: 703:. 679:: 673:7 650:. 630:: 624:5 340:) 322:( 275:. 253:; 189:( 145:. 126:. 20:)

Index

Membrane proteins

photosynthesis
thylakoid
proteins
biological membranes
cell membrane
transmembrane
integral monotopic
Peripheral membrane proteins
protein structures
native
conformation of the protein
Membrane receptor
internal
external
Transport proteins
ions
Transporter Classification database
enzymes
oxidoreductase
transferase
hydrolase
Cell adhesion molecules
immune response
hydrophobicity analyses
hydrophobic
amino acid

transmembrane proteins

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