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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".
354:, and other non-covalent interactions. Peripheral proteins dissociate following treatment with a polar reagent, such as a solution with an elevated 652:"Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin" 46:. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a 2015: 1828: 1765:- Database of 3D structures of integral membrane proteins and hydrophobic peptides with an emphasis on crystallization conditions 70:
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).
518: 506: 362: 313: 304: 155: 152: 19: 1722:, a comprehensive classification of transmembrane transporter proteins 300: 183: 175: 1980: 407: 403: 206: 131: 94: 28: 1532: 769: 620: 2163: 2113: 1933: 1871: 410:, are sometimes considered a separate category. These proteins are 1943: 1938: 1837: 650:
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
1778:- A curated list of selected transmembrane proteins from the 1490:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Carpenter EP, Beis K, Cameron AD, Iwata S (October 2008).
1787:- a database of membrane protein structures simulated by 1282: 108: 54:) or associate with one or the other side of a membrane ( 1698: 843:
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
499: 2023: 62:are transiently associated with the cell membrane. 709:Biochimica et Biophysica Acta (BBA) - Biomembranes 450:, are common. It is estimated that 20–30% of all 1398:"Membrane proteins: always an insoluble problem?" 2176: 1235:"Elucidating the Structure of Membrane Proteins" 1699:Membrane Protein Structural Dynamics Consortium 1056:"Dissecting the Structure of Membrane Proteins" 283: 151:of protein sequences, i.e. the localization of 1596: 754:(December 2006). "Membrane-protein topology". 600: 598: 579:(TransMembrane Protein Helix-Packing Database) 2009: 1822: 1709: 1633: 161: 1746:approximately arranged in the lipid bilayer. 1232: 1061:Genetic Engineering & Biotechnology News 346:or to integral proteins by a combination of 238:proteins, which are present in all types of 1740:Protein Data Bank of Transmembrane Proteins 1378:on 2020-08-04 – via Semantic Scholar. 939: 798: 595: 307:loop 3. interaction by a covalently bound 188:The membrane is represented in light-brown. 2016: 2002: 1829: 1815: 836: 750: 93:proteins relay signals between the cell's 78:in isolation from its native environment. 1669: 1616: 1570: 1560: 1509: 1423: 1308: 1252: 1053: 1030: 979: 915: 905: 860: 720: 679: 669: 1395: 1233:Martin, Joseph; Sawyer, Abigail (2019). 513:can be used to render membrane proteins 287: 165: 18: 792: 342:are temporarily attached either to the 50:and can either penetrate the membrane ( 2177: 757:Nature Reviews. Molecular Cell Biology 1997: 1810: 1289:Current Opinion in Structural Biology 1228: 1226: 1224: 1222: 1220: 1218: 1157: 380: 733:– via Elsevier Science Direct. 42:that are part of, or interact with, 1720:Transporter Classification database 406:, and certain proteins involved in 113:Transporter Classification database 13: 1652:10.1016/b978-0-12-417027-8.00003-9 1590: 1215: 1047: 248:proteins, which are found only in 122:may have many activities, such as 14: 2196: 1687: 500:Purification of membrane proteins 1692: 1403:Biochemical Society Transactions 1381: 1268: 1207: 1149: 1094:, Sonnhammer EL (January 2001). 931: 736: 438:Membrane proteins, like soluble 1857:Post-translational modification 1597:Johnson JE, Cornell RB (1999). 1526: 1477: 1440: 1389: 1325: 1276: 1080: 552:Inner nuclear membrane proteins 1634:Alenghat FJ, Golan DE (2013). 1247:(4). Future Science: 167–170. 1054:Liszewski K (1 October 2015). 996: 881: 744: 696: 643: 608:Nature Reviews. Drug Discovery 23:Membrane protein complexes of 1: 1736:arranged in the lipid bilayer 589: 471: 433: 358:or high salt concentrations. 1836: 1803:from several model organisms 1734:peripheral membrane proteins 1502:10.1016/j.bbapap.2013.06.003 1341:Journal of Molecular Biology 1104:Journal of Molecular Biology 862:10.1016/j.bbamcr.2013.10.009 722:10.1016/j.bbamem.2013.03.003 567:List of MeSH codes (D12.776) 414:but can undergo significant 340:Peripheral membrane proteins 284:Peripheral membrane proteins 174:: 1. a single transmembrane 170:Schematic representation of 60:Peripheral membrane proteins 7: 2094:Peripheral membrane protein 1799:provides information about 1640:Current Topics in Membranes 534: 468:encodes membrane proteins. 335:Peripheral membrane protein 277:Integral monotopic proteins 226:Integral polytopic proteins 81: 76:conformation of the protein 10: 2201: 2085:Integral membrane proteins 1898:Protein structural domains 1710:Membrane protein databases 1604:Molecular Membrane Biology 1142:on 2020-08-04 – via 1017:(Database issue): D310-4. 480:of over 50% of all modern 476:Membrane proteins are the 384: 332: 203:Integral membrane proteins 191: 162:Integral membrane proteins 2106: 2070: 2032: 1911: 1885: 1844: 1396:Rawlings AE (June 2016). 1301:10.1016/j.sbi.2008.07.001 972:10.1038/s41586-018-0061-y 907:10.1186/s12915-017-0404-4 256:, and outer membranes of 194:Integral membrane protein 180:bitopic membrane protein 2129:Lipid raft/microdomains 1618:10.1080/096876899294544 1562:10.1073/pnas.0811089106 1186:10.1126/science.1109730 572:Receptor (biochemistry) 525:Affinity chromatography 426:or reversibly with the 317:) 4. electrostatic or 296:: 1. interaction by an 149:hydrophobicity analyses 138:Cell adhesion molecules 2134:Membrane contact sites 2098:Lipid-anchored protein 2080:Membrane glycoproteins 1744:transmembrane proteins 1353:10.1006/jmbi.2000.4315 1117:10.1006/jmbi.2000.4315 1010:Nucleic Acids Research 671:10.1186/1741-7007-7-50 583:Transmembrane proteins 416:conformational changes 396:antibacterial peptides 330: 321:with membrane lipids ( 254:Gram-negative bacteria 230:transmembrane topology 189: 172:transmembrane proteins 32: 2089:transmembrane protein 1961:Photoreceptor protein 1254:10.2144/btn-2019-0030 873:– via Elsevier 291: 198:Transmembrane protein 169: 22: 2114:Caveolae/Coated pits 1852:Protein biosynthesis 1463:10.1038/nbt1188-1321 1450:Nature Biotechnology 1074:10.1089/gen.35.17.02 1068:(17): 1, 14, 16–17. 799:Gerald Karp (2009). 420:oligomeric complexes 240:biological membranes 44:biological membranes 1797:Membranome database 1728:- 3D structures of 1553:2009PNAS..10611925C 1416:10.1042/BST20160025 1178:2005Sci...308.1321D 1023:10.1093/nar/gkt1242 964:2018Natur.557..123S 809:John Wiley and Sons 542:Annular lipid shell 448:disordered proteins 107:move molecules and 2139:Membrane nanotubes 2024:Structures of the 1792:molecular dynamics 1774:2013-12-25 at the 1761:2020-08-03 at the 562:Ion pump (biology) 387:Pore-forming toxin 381:Polypeptide toxins 331: 319:ionic interactions 190: 105:Transport proteins 68:protein structures 56:integral monotopic 33: 2185:Membrane proteins 2172: 2171: 2072:Membrane proteins 1991: 1990: 1893:Protein structure 1867:Protein targeting 1780:Protein Data Bank 1457:(11): 1321–1325. 958:(7703): 123–126. 818:978-0-470-48337-4 811:. pp. 128–. 529:polyhistidine-tag 440:globular proteins 211:nonpolar solvents 91:Membrane receptor 36:Membrane proteins 2192: 2154:Nuclear envelope 2149:Nodes of Ranvier 2018: 2011: 2004: 1995: 1994: 1971:Phycobiliprotein 1929:Globular protein 1924:Membrane protein 1919:List of proteins 1831: 1824: 1817: 1808: 1807: 1801:bitopic proteins 1769:Mpstruc database 1683: 1673: 1630: 1620: 1585: 1584: 1574: 1564: 1547:(29): 11925–30. 1530: 1524: 1523: 1513: 1481: 1475: 1474: 1444: 1438: 1437: 1427: 1393: 1387: 1386: 1385: 1379: 1377: 1371:. Archived from 1338: 1329: 1323: 1322: 1312: 1280: 1274: 1273: 1272: 1266: 1256: 1230: 1213: 1212: 1211: 1205: 1172:(5726): 1321–3. 1161: 1155: 1154: 1153: 1147: 1144:Semantic Scholar 1141: 1135:. Archived from 1100: 1084: 1078: 1077: 1051: 1045: 1044: 1034: 1000: 994: 993: 983: 943: 937: 936: 935: 929: 919: 909: 885: 879: 878: 864: 840: 834: 833: 827: 825: 806: 796: 790: 789: 748: 742: 741: 740: 734: 724: 700: 694: 693: 683: 673: 647: 641: 640: 602: 444:fibrous proteins 394:toxins and many 270:Bitopic proteins 2200: 2199: 2195: 2194: 2193: 2191: 2190: 2189: 2175: 2174: 2173: 2168: 2102: 2066: 2034:Membrane lipids 2028: 2022: 1992: 1987: 1951:Fibrous protein 1907: 1881: 1877:Protein methods 1862:Protein folding 1840: 1835: 1776:Wayback Machine 1763:Wayback Machine 1742:- 3D models of 1712: 1695: 1690: 1662: 1593: 1591:Further reading 1588: 1531: 1527: 1496:(10): 2045–56. 1482: 1478: 1445: 1441: 1394: 1390: 1380: 1375: 1336: 1330: 1326: 1281: 1277: 1267: 1243:(Print issue). 1231: 1216: 1206: 1162: 1158: 1148: 1139: 1098: 1085: 1081: 1052: 1048: 1001: 997: 944: 940: 930: 886: 882: 841: 837: 823: 821: 819: 797: 793: 770:10.1038/nrm2063 749: 745: 735: 701: 697: 648: 644: 621:10.1038/nrd2199 603: 596: 592: 587: 547:Carrier protein 537: 502: 494:cystic fibrosis 482:medicinal drugs 474: 436: 389: 383: 337: 286: 250:outer membranes 213:, or sometimes 200: 192:Main articles: 187: 164: 142:immune response 84: 17: 12: 11: 5: 2198: 2188: 2187: 2170: 2169: 2167: 2166: 2161: 2159:Phycobilisomes 2156: 2151: 2146: 2141: 2136: 2131: 2126: 2121: 2119:Cell junctions 2116: 2110: 2108: 2104: 2103: 2101: 2100: 2091: 2082: 2076: 2074: 2068: 2067: 2065: 2064: 2059: 2054: 2049: 2044: 2038: 2036: 2030: 2029: 2021: 2020: 2013: 2006: 1998: 1989: 1988: 1986: 1985: 1984: 1983: 1978: 1973: 1963: 1958: 1953: 1948: 1947: 1946: 1941: 1936: 1926: 1921: 1915: 1913: 1909: 1908: 1906: 1905: 1900: 1895: 1889: 1887: 1883: 1882: 1880: 1879: 1874: 1869: 1864: 1859: 1854: 1848: 1846: 1842: 1841: 1834: 1833: 1826: 1819: 1811: 1805: 1804: 1794: 1789:coarse-grained 1782: 1766: 1753: 1747: 1737: 1723: 1711: 1708: 1707: 1706: 1701: 1694: 1691: 1689: 1688:External links 1686: 1685: 1684: 1660: 1631: 1592: 1589: 1587: 1586: 1525: 1476: 1439: 1388: 1324: 1275: 1214: 1156: 1079: 1046: 995: 938: 880: 875:Science Direct 855:(8): 1542–50. 835: 817: 791: 764:(12): 909–18. 743: 695: 642: 593: 591: 588: 586: 585: 580: 574: 569: 564: 559: 554: 549: 544: 538: 536: 533: 501: 498: 473: 470: 435: 432: 422:and associate 385:Main article: 382: 379: 367:diacylglycerol 333:Main article: 309:membrane lipid 285: 282: 281: 280: 274: 267: 266: 265: 243: 163: 160: 145: 144: 135: 124:oxidoreductase 116: 102: 83: 80: 25:photosynthesis 15: 9: 6: 4: 3: 2: 2197: 2186: 2183: 2182: 2180: 2165: 2162: 2160: 2157: 2155: 2152: 2150: 2147: 2145: 2144:Myelin sheath 2142: 2140: 2137: 2135: 2132: 2130: 2127: 2125: 2122: 2120: 2117: 2115: 2112: 2111: 2109: 2105: 2099: 2095: 2092: 2090: 2086: 2083: 2081: 2078: 2077: 2075: 2073: 2069: 2063: 2060: 2058: 2057:Sphingolipids 2055: 2053: 2050: 2048: 2047:Phospholipids 2045: 2043: 2042:Lipid bilayer 2040: 2039: 2037: 2035: 2031: 2027: 2026:cell membrane 2019: 2014: 2012: 2007: 2005: 2000: 1999: 1996: 1982: 1979: 1977: 1974: 1972: 1969: 1968: 1967: 1964: 1962: 1959: 1957: 1956:Chromoprotein 1954: 1952: 1949: 1945: 1942: 1940: 1937: 1935: 1932: 1931: 1930: 1927: 1925: 1922: 1920: 1917: 1916: 1914: 1910: 1904: 1901: 1899: 1896: 1894: 1891: 1890: 1888: 1884: 1878: 1875: 1873: 1870: 1868: 1865: 1863: 1860: 1858: 1855: 1853: 1850: 1849: 1847: 1843: 1839: 1832: 1827: 1825: 1820: 1818: 1813: 1812: 1809: 1802: 1798: 1795: 1793: 1790: 1786: 1783: 1781: 1777: 1773: 1770: 1767: 1764: 1760: 1757: 1754: 1751: 1748: 1745: 1741: 1738: 1735: 1731: 1727: 1724: 1721: 1717: 1714: 1713: 1705: 1702: 1700: 1697: 1696: 1693:Organizations 1681: 1677: 1672: 1667: 1663: 1661:9780124170278 1657: 1653: 1649: 1645: 1641: 1637: 1632: 1628: 1624: 1619: 1614: 1611:(3): 217–35. 1610: 1606: 1605: 1600: 1595: 1594: 1582: 1578: 1573: 1568: 1563: 1558: 1554: 1550: 1546: 1542: 1541: 1536: 1529: 1521: 1517: 1512: 1507: 1503: 1499: 1495: 1491: 1487: 1480: 1472: 1468: 1464: 1460: 1456: 1452: 1451: 1443: 1435: 1431: 1426: 1421: 1417: 1413: 1409: 1405: 1404: 1399: 1392: 1384: 1374: 1370: 1366: 1362: 1358: 1354: 1350: 1347:(3): 567–80. 1346: 1342: 1335: 1328: 1320: 1316: 1311: 1306: 1302: 1298: 1294: 1290: 1286: 1279: 1271: 1264: 1260: 1255: 1250: 1246: 1242: 1241: 1240:BioTechniques 1237:. Tech News. 1236: 1229: 1227: 1225: 1223: 1221: 1219: 1210: 1203: 1199: 1195: 1191: 1187: 1183: 1179: 1175: 1171: 1167: 1160: 1152: 1145: 1138: 1134: 1130: 1126: 1122: 1118: 1114: 1111:(3): 567–80. 1110: 1106: 1105: 1097: 1093: 1090:, Larsson B, 1089: 1083: 1075: 1071: 1067: 1063: 1062: 1057: 1050: 1042: 1038: 1033: 1028: 1024: 1020: 1016: 1012: 1011: 1006: 999: 991: 987: 982: 977: 973: 969: 965: 961: 957: 953: 949: 942: 934: 927: 923: 918: 913: 908: 903: 899: 895: 891: 884: 876: 872: 868: 863: 858: 854: 850: 846: 839: 831: 820: 814: 810: 805: 804: 795: 787: 783: 779: 775: 771: 767: 763: 759: 758: 753: 747: 739: 732: 728: 723: 718: 715:(8): 1690–9. 714: 710: 706: 699: 691: 687: 682: 677: 672: 667: 663: 659: 658: 653: 646: 638: 634: 630: 626: 622: 618: 615:(12): 993–6. 614: 610: 609: 601: 599: 594: 584: 581: 578: 575: 573: 570: 568: 565: 563: 560: 558: 555: 553: 550: 548: 545: 543: 540: 539: 532: 530: 526: 522: 520: 516: 515:water-soluble 512: 508: 497: 495: 491: 487: 486:heart disease 483: 479: 469: 467: 463: 462: 457: 453: 449: 445: 441: 431: 429: 428:lipid bilayer 425: 421: 417: 413: 412:water-soluble 409: 405: 401: 397: 393: 388: 378: 376: 372: 368: 364: 359: 357: 353: 352:electrostatic 349: 345: 344:lipid bilayer 341: 336: 328: 324: 320: 316: 315: 310: 306: 302: 299: 295: 294:cell membrane 290: 278: 275: 271: 268: 263: 259: 255: 251: 247: 244: 241: 237: 234: 233: 231: 227: 224: 223: 222: 220: 216: 212: 208: 204: 199: 195: 185: 181: 177: 173: 168: 159: 157: 154: 150: 143: 139: 136: 133: 129: 125: 121: 117: 114: 110: 106: 103: 101:environments. 100: 96: 92: 89: 88: 87: 79: 77: 73: 69: 63: 61: 57: 53: 52:transmembrane 49: 48:cell membrane 45: 41: 37: 30: 26: 21: 2071: 2052:Lipoproteins 1923: 1756:Membrane PDB 1643: 1639: 1608: 1602: 1544: 1538: 1528: 1493: 1489: 1479: 1454: 1448: 1442: 1410:(3): 790–5. 1407: 1401: 1391: 1373:the original 1344: 1340: 1327: 1295:(5): 581–6. 1292: 1288: 1278: 1244: 1238: 1169: 1165: 1159: 1137:the original 1108: 1102: 1092:von Heijne G 1082: 1065: 1059: 1049: 1014: 1008: 998: 955: 951: 941: 897: 893: 883: 852: 848: 838: 830:Google Books 828:– via 822:. Retrieved 802: 794: 761: 755: 752:von Heijne G 746: 712: 708: 698: 661: 655: 645: 612: 606: 523: 503: 475: 459: 437: 424:irreversibly 390: 360: 338: 322: 312: 262:chloroplasts 258:mitochondria 236:Helix bundle 201: 146: 85: 64: 35: 34: 1976:Phytochrome 1966:Biliprotein 1750:TransportDB 894:BMC Biology 824:13 November 657:BMC Biology 611:(Opinion). 557:Ion channel 519:hydrophilic 507:hydrophobic 490:Alzheimer's 392:Polypeptide 373:chains, or 348:hydrophobic 327:calcium ion 305:hydrophobic 298:amphipathic 246:Beta barrel 158:sequences. 153:hydrophobic 128:transferase 38:are common 2124:Glycocalyx 1903:Proteasome 1886:Structures 1646:: 89–120. 1168:(Report). 590:References 511:Detergents 472:In disease 434:In genomes 404:hemolysins 398:, such as 363:fatty acid 325:through a 314:lipidation 215:denaturing 207:detergents 156:amino acid 2164:Porosomes 1981:Lipocalin 1845:Processes 1785:MemProtMD 1064:(paper). 900:(1): 66. 408:apoptosis 273:proteins. 132:hydrolase 118:Membrane 29:thylakoid 2179:Category 1934:Globulin 1872:Proteome 1838:Proteins 1772:Archived 1759:Archived 1730:integral 1680:24210428 1627:10503244 1581:19581598 1520:23777860 1434:27284043 1369:15769874 1361:11152613 1319:18674618 1263:30987442 1194:15919996 1133:15769874 1125:11152613 1041:24293656 990:29695868 926:28738801 871:24135059 786:22218266 778:17139331 731:23500619 690:19678920 637:11979420 629:17139284 535:See also 454:in most 400:colicins 186:protein 99:external 95:internal 82:Function 40:proteins 31:membrane 2062:Sterols 1944:Albumin 1939:Edestin 1671:4193470 1572:2715541 1549:Bibcode 1511:3779079 1471:9518666 1425:4900757 1310:2580798 1202:6942424 1174:Bibcode 1166:Science 1088:Krogh A 1032:3964979 981:6004266 960:Bibcode 917:5525207 681:2739160 478:targets 461:E. coli 456:genomes 418:, form 301:α-helix 219:bilayer 184:β-sheet 176:α-helix 120:enzymes 27:in the 1678:  1668:  1658:  1625:  1579:  1569:  1518:  1508:  1469:  1432:  1422:  1367:  1359:  1317:  1307:  1261:  1200:  1192:  1131:  1123:  1039:  1029:  988:  978:  952:Nature 924:  914:  869:  815:  784:  776:  729:  688:  678:  664:: 50. 635:  627:  466:genome 446:, and 371:prenyl 72:native 2107:Other 1912:Types 1467:S2CID 1376:(PDF) 1365:S2CID 1337:(PDF) 1198:S2CID 1140:(PDF) 1129:S2CID 1099:(PDF) 782:S2CID 633:S2CID 577:TMPad 452:genes 1732:and 1716:TCDB 1676:PMID 1656:ISBN 1623:PMID 1577:PMID 1516:PMID 1494:1834 1430:PMID 1357:PMID 1315:PMID 1259:PMID 1190:PMID 1121:PMID 1037:PMID 986:PMID 922:PMID 867:PMID 853:1843 826:2010 813:ISBN 774:PMID 727:PMID 713:1828 686:PMID 625:PMID 492:and 323:e.g. 260:and 196:and 109:ions 97:and 1666:PMC 1648:doi 1613:doi 1567:PMC 1557:doi 1545:106 1506:PMC 1498:doi 1459:doi 1420:PMC 1412:doi 1349:doi 1345:305 1305:PMC 1297:doi 1249:doi 1182:doi 1170:308 1113:doi 1109:305 1070:doi 1027:PMC 1019:doi 976:PMC 968:doi 956:557 912:PMC 902:doi 857:doi 766:doi 717:doi 676:PMC 666:doi 617:doi 402:or 375:GPI 369:or 252:of 130:or 58:). 2181:: 1718:- 1674:. 1664:. 1654:. 1644:72 1642:. 1638:. 1621:. 1609:16 1607:. 1601:. 1575:. 1565:. 1555:. 1543:. 1537:. 1514:. 1504:. 1492:. 1488:. 1465:. 1453:. 1428:. 1418:. 1408:44 1406:. 1400:. 1363:. 1355:. 1343:. 1339:. 1313:. 1303:. 1293:18 1291:. 1287:. 1257:. 1245:66 1217:^ 1196:. 1188:. 1180:. 1127:. 1119:. 1107:. 1101:. 1066:35 1058:. 1035:. 1025:. 1015:42 1013:. 1007:. 984:. 974:. 966:. 954:. 950:. 920:. 910:. 898:15 896:. 892:. 865:. 851:. 847:. 807:. 780:. 772:. 760:. 725:. 711:. 707:. 684:. 674:. 660:. 654:. 631:. 623:. 597:^ 496:. 488:, 442:, 430:. 365:, 356:pH 350:, 221:: 209:, 126:, 74:) 2096:/ 2087:/ 2017:e 2010:t 2003:v 1830:e 1823:t 1816:v 1682:. 1650:: 1629:. 1615:: 1583:. 1559:: 1551:: 1522:. 1500:: 1473:. 1461:: 1455:6 1436:. 1414:: 1351:: 1321:. 1299:: 1265:. 1251:: 1204:. 1184:: 1176:: 1146:. 1115:: 1076:. 1072:: 1043:. 1021:: 992:. 970:: 962:: 928:. 904:: 877:. 859:: 832:. 788:. 768:: 762:7 719:: 692:. 668:: 662:7 639:. 619:: 613:5 329:) 311:( 264:. 242:; 178:( 134:. 115:.

Index


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
α-helix

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