230:
212:). Type II and III are anchored with a signal-anchor sequence, with type II being targeted to the ER lumen with its C-terminal domain, while type III have their N-terminal domains targeted to the ER lumen. Type IV is subdivided into IV-A, with their N-terminal domains targeted to the cytosol and IV-B, with an N-terminal domain targeted to the lumen. The implications for the division in the four types are especially manifest at the time of translocation and ER-bound translation, when the protein has to be passed through the ER membrane in a direction dependent on the type.
216:
389:), because its polar residues can face the central water-filled channel of the translocon. Such mechanism is necessary for incorporation of polar α-helices into structures of transmembrane proteins. The amphiphilic helices remain attached to the translocon until the protein is completely synthesized and folded. If the protein remains unfolded and attached to the translocon for too long, it is degraded by specific "quality control" cellular systems.
275:
these proteins is more difficult than globular proteins. As of
January 2013 less than 0.1% of protein structures determined were membrane proteins despite being 20–30% of the total proteome. Due to this difficulty and the importance of this class of proteins methods of protein structure prediction based on hydropathy plots, the positive inside rule and other methods have been developed.
406:, such as protein Skp. It is thought that β-barrel membrane proteins come from one ancestor even having different number of sheets which could be added or doubled during evolution. Some studies show a huge sequence conservation among different organisms and also conserved amino acids which hold the structure and help with folding.
20:
274:
which have hydrophobic surfaces, are relatively flexible and are expressed at relatively low levels. This creates difficulties in obtaining enough protein and then growing crystals. Hence, despite the significant functional importance of membrane proteins, determining atomic resolution structures for
219:
Group I and II transmembrane proteins have opposite final topologies. Group I proteins have the N terminus on the far side and C terminus on the cytosolic side. Group II proteins have the C terminus on the far side and N terminus in the cytosol. However final topology not the only criterion for
385:. The translocon channel provides a highly heterogeneous environment for the nascent transmembrane α-helices. A relatively polar amphiphilic α-helix can adopt a transmembrane orientation in the translocon (although it would be at the membrane surface or unfolded
397:
Stability of beta barrel (β-barrel) transmembrane proteins is similar to stability of water-soluble proteins, based on chemical denaturation studies. Some of them are very stable even in chaotropic agents and high temperature. Their folding
127:. This is the major category of transmembrane proteins. In humans, 27% of all proteins have been estimated to be alpha-helical membrane proteins. Beta-barrel proteins are so far found only in outer membranes of
808:
1243:
Nicholson, L. K.; Cross, T. A. (1989). "Gramicidin cation channel: an experimental determination of the right-handed helix sense and verification of .beta.-type hydrogen bonding".
357:
micelles has four transmembrane α-helices folded, while the rest of the protein is situated at the micelle-water interface and can adopt different types of non-native
1699:
Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF (November 2002). "Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling".
361:
structures. Free energy differences between such detergent-denatured and native states are similar to stabilities of water-soluble proteins (< 10 kcal/mol).
155:. All beta-barrel transmembrane proteins have simplest up-and-down topology, which may reflect their common evolutionary origin and similar folding mechanism.
586:
200:. Type I transmembrane proteins are anchored to the lipid membrane with a stop-transfer anchor sequence and have their N-terminal domains targeted to the
914:
transporter BtuB, Fe(III)-pyochelin receptor FptA, receptor FepA, ferric hydroxamate uptake receptor FhuA, transporter FecA, and pyoverdine receptor FpvA
639:
1750:
Murzin AG, Lesk AM, Chothia C (March 1994). "Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis".
796:
174:
has not been reported in natural proteins. Nonetheless, this structure was experimentally observed in specifically designed artificial peptides.
1194:"Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin"
123:. Alpha-helical proteins are present in the inner membranes of bacterial cells or the plasma membrane of eukaryotic cells, and sometimes in the
1640:
Michalik, Marcin; Orwick-Rydmark, Marcella; Habeck, Michael; Alva, Vikram; Arnold, Thomas; Linke, Dirk; Permyakov, Eugene A. (3 August 2017).
220:
defining transmembrane protein groups, rather location of topogenic determinants and mechanism of assembly is considered in the classification
837:
308:
studies, because they do not unfold completely within the membranes (the complete unfolding would require breaking down too many α-helical
1423:
White, Stephen. "General
Principle of Membrane Protein Folding and Stability". Stephen White Laboratory Homepage. 10 Nov. 2009. web.
1802:
678:
Outer membrane auxiliary proteins (polysaccharide transporter) - α-helical transmembrane proteins from the outer bacterial membrane
965:
345:
experiments. This state represents a combination of folded hydrophobic α-helices and partially unfolded segments covered by the
633:
1152:
1118:
1971:
472:
415:
158:
In addition to the protein domains, there are unusual transmembrane elements formed by peptides. A typical example is
615:
Drug/Metabolite
Transporter (small multidrug resistance transporter EmrE - the structures are retracted as erroneous)
1482:
484:
1589:
Hopf, Thomas A.; Colwell, Lucy J.; Sheridan, Robert; Rost, Burkhard; Sander, Chris; Marks, Debora S. (June 2012).
889:
802:
975:
903:
851:
790:
441:
1340:
Goder, Veit; Spiess, Martin (31 August 2001). "Topogenesis of membrane proteins: determinants and dynamics".
978:, also known as trimeric outer membrane factors (n=12,S=18) including TolC and multidrug resistance proteins
373:
is technically difficult. There are relatively few examples of the successful refolding experiments, as for
1795:
1507:
Elofsson, Arne; Heijne, Gunnar von (7 June 2007). "Membrane
Protein Structure: Prediction versus Reality".
644:
140:
91:
24:
1880:
929:
917:
342:
305:
72:
229:
1080:
Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter (2002).
755:
253:
99:
52:
1871:
879:
625:
79:
44:
1642:"An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins"
1566:
1521:
934:
899:
771:
654:
492:
451:
124:
1788:
760:
488:
90:. Depending on the number of transmembrane segments, transmembrane proteins can be classified as
1884:
1866:
1561:
1516:
1012:
827:
814:
662:
649:
476:
354:
167:
163:
136:
128:
102:, meaning that they are also permanently attached to the membrane, but do not pass through it.
1142:
1920:
1552:
Chen, Chien Peter; Rost, Burkhard (2002). "State-of-the-art in membrane protein prediction".
1530:
1108:
819:
688:
590:
241:
201:
1433:
Carpenter, Elisabeth P; Beis, Konstantinos; Cameron, Alexander D; Iwata, So (October 2008).
1280:"Bilayer thickness determines the alignment of model polyproline helices in lipid membranes"
1708:
1653:
1291:
1007:
743:
594:
498:
298:
83:
381:, all such proteins are normally folded co-translationally within the large transmembrane
8:
403:
265:
245:
1712:
1657:
1295:
324:, or unfolding of peripheral regions and nonregular loops that are locally less stable.
1732:
1676:
1641:
1617:
1590:
1459:
1434:
1401:
1376:
1220:
1193:
1057:
1032:
152:
1353:
215:
1925:
1767:
1763:
1724:
1681:
1622:
1571:
1534:
1464:
1406:
1357:
1309:
1260:
1225:
1148:
1114:
1062:
1002:
765:
749:
732:
719:
693:
629:
554:
480:
426:
374:
350:
288:
183:
171:
1736:
162:, a peptide that forms a dimeric transmembrane β-helix. This peptide is secreted by
1940:
1858:
1759:
1716:
1671:
1661:
1612:
1602:
1526:
1454:
1446:
1396:
1388:
1349:
1299:
1252:
1215:
1205:
1052:
1044:
673:
658:
606:
271:
264:. The portion of the membrane proteins that are attached to the lipid bilayer (see
249:
237:
189:
95:
56:
1780:
1278:
Kubyshkin, Vladimir; Grage, Stephan L.; Ulrich, Anne S.; Budisa, Nediljko (2019).
1935:
1666:
869:
855:
712:
574:
548:
321:
284:
205:
197:
87:
55:
of specific substances across the membrane. They frequently undergo significant
1820:
1607:
1392:
1081:
698:
532:
329:
317:
209:
1450:
392:
208:
during synthesis (and the extracellular space, if mature forms are located on
1965:
1945:
1905:
1828:
1812:
571:
539:
193:
48:
19:
1720:
1033:"Environment Polarity in Proteins Mapped Noninvasively by FTIR Spectroscopy"
953:
are, respectively, the number of beta-strands and the "shear number" of the
31:) 2) a multipass membrane protein (α-helix) 3) a multipass membrane protein
1843:
1833:
1728:
1685:
1626:
1591:"Three-Dimensional Structures of Membrane Proteins from Genomic Sequencing"
1575:
1538:
1468:
1410:
1361:
1313:
1229:
1210:
1179:
1066:
506:
459:
257:
159:
148:
144:
1771:
1264:
1838:
1375:
Cross, Timothy A.; Sharma, Mukesh; Yi, Myunggi; Zhou, Huan-Xiang (2011).
954:
725:
579:
Major
Facilitator Superfamily (Glycerol-3-phosphate transporter, Lactose
445:
358:
301:
261:
120:
116:
68:
60:
28:
1486:
1256:
1915:
1910:
1377:"Influence of Solubilizing Environments on Membrane Protein Structures"
1304:
1279:
981:
865:
841:
558:
543:
382:
32:
1048:
959:
777:
600:
Dicarboxylate/amino acid:cation symporter (proton glutamate symporter)
911:
809:
Antimicrobial peptide resistance and lipid A acylation protein family
783:
Beta barrels from eight beta-strands and with "shear number" of ten (
668:
603:
Monovalent cation/proton antiporter (Sodium/proton antiporter 1 NhaA)
430:
346:
132:
64:
293:
1950:
1900:
925:
705:
580:
502:
455:
338:
233:
Increase in the number of 3D structures of membrane proteins known
59:
to move a substance through the membrane. They are usually highly
1175:
312:
in the nonpolar media). On the other hand, these proteins easily
1639:
1191:
619:
565:
512:
316:, due to non-native aggregation in membranes, transition to the
304:(α-helical) proteins are unusually stable judging from thermal
1930:
1848:
1435:"Overcoming the challenges of membrane protein crystallography"
519:
309:
190:
position of the protein N- and C-termini on the different sides
364:
1031:
Manor, Joshua; Feldblum, Esther S.; Arkin, Isaiah T. (2012).
738:
434:
67:
or nonpolar solvents for extraction, although some of them (
393:
Stability and folding of beta-barrel transmembrane proteins
1277:
1192:
Almén MS, Nordström KJ, Fredriksson R, Schiöth HB (2009).
525:
1698:
1432:
94:, or as multipass membrane proteins. Some other integral
86:, is largely hydrophobic and can be visualized using the
23:
Schematic representation of transmembrane proteins: 1) a
1588:
1079:
420:
278:
645:
Small-conductance mechanosensitive ion channel (MscS)
465:
115:
There are two basic types of transmembrane proteins:
63:
and aggregate and precipitate in water. They require
1810:
960:
Beta-barrels composed of several polypeptide chains
778:
Beta-barrels composed of a single polypeptide chain
1174:alpha-helical proteins in outer membranes include
1030:
1749:
1374:
1106:
906:. They are ligand-gated outer membrane channels (
518:Proton or sodium translocating F-type and V-type
294:Stability of alpha-helical transmembrane proteins
1963:
706:Proteins with single transmembrane alpha-helices
640:Large-conductance mechanosensitive channel, MscL
797:Virulence-related outer membrane protein family
1506:
1242:
369:Refolding of α-helical transmembrane proteins
110:
35:. The membrane is represented in light yellow.
1796:
1147:. Cambridge University Press. pp. 208–.
620:Alpha-helical channels including ion channels
566:Porters (uniporters, symporters, antiporters)
513:Electrochemical potential-driven transporters
268:) consist mostly of hydrophobic amino acids.
177:
16:Protein spanning across a biological membrane
1692:
838:FadL outer membrane protein transport family
327:It is also important to properly define the
1339:
365:Folding of α-helical transmembrane proteins
1803:
1789:
1100:
1086:Molecular Biology of the Cell. 4th edition
471:Transmembrane cytochrome b-like proteins:
51:. Many transmembrane proteins function as
1675:
1665:
1616:
1606:
1565:
1520:
1483:"Membrane Proteins of known 3D Structure"
1458:
1400:
1303:
1219:
1209:
1140:
1056:
1037:The Journal of Physical Chemistry Letters
1551:
1531:10.1146/annurev.biochem.76.052705.163539
1134:
228:
214:
18:
1073:
526:P-P-bond hydrolysis-driven transporters
1964:
634:inward-rectifier potassium ion channel
341:is different from that in the thermal
1784:
1439:Current Opinion in Structural Biology
1417:
701:formation protein (DsbA-DsbB complex)
479:; formate dehydrogenase, respiratory
421:Light absorption-driven transporters
256:of these proteins are transmembrane
1284:Physical Chemistry Chemical Physics
587:Resistance-nodulation-cell division
473:coenzyme Q - cytochrome c reductase
416:Transporter Classification Database
279:Thermodynamic stability and folding
13:
466:Oxidoreduction-driven transporters
337:of membrane proteins in detergent
188:This classification refers to the
14:
1983:
766:Corticosteroid 11β-dehydrogenases
583:, and Multidrug transporter EmrD)
1113:. Academic Press. pp. 37–.
992:) . These proteins are secreted.
485:succinate - coenzyme Q reductase
409:
402:is facilitated by water-soluble
320:states, formation of non-native
240:structures can be determined by
82:that spans the membrane, or the
53:gateways to permit the transport
1743:
1633:
1582:
1545:
1500:
1475:
1426:
1368:
1333:
924:) that includes outer membrane
890:Outer membrane phospholipase A1
803:Outer membrane protein W family
442:photosynthetic reaction centres
224:
47:that spans the entirety of the
1381:Trends in Biochemical Sciences
1320:
1271:
1236:
1185:
1168:
1024:
976:Outer membrane efflux proteins
852:General bacterial porin family
791:OmpA-like transmembrane domain
535:(five different conformations)
349:. For example, the "unfolded"
196:. Types I, II, III and IV are
71:) can be also extracted using
1:
1509:Annual Review of Biochemistry
1354:10.1016/S0014-5793(01)02712-0
1018:
561:(preprotein translocase SecY)
92:single-pass membrane proteins
1764:10.1016/0022-2836(94)90064-7
1667:10.1371/journal.pone.0182016
988:) and α-hemolysin (heptamer
930:adhesin/invasin OpcA protein
25:single-pass membrane protein
7:
1881:Peripheral membrane protein
996:
918:Outer membrane protein OpcA
650:CorA metal ion transporters
111:Classification by structure
10:
1988:
1972:Integral membrane proteins
1872:Integral membrane proteins
1608:10.1016/j.cell.2012.04.012
1393:10.1016/j.tibs.2010.07.005
1107:Steven R. Goodman (2008).
756:Fatty acid amide hydrolase
682:
538:Calcium ATPase regulators
487:(fumarate reductase); and
452:Light-harvesting complexes
413:
282:
181:
178:Classification by topology
1893:
1857:
1819:
1451:10.1016/j.sbi.2008.07.001
880:Nucleoside-specific porin
626:Voltage-gated ion channel
429:-like proteins including
45:integral membrane protein
1144:Essential bioinformatics
966:Trimeric autotransporter
935:Outer membrane protein G
900:TonB-dependent receptors
772:Signal Peptide Peptidase
761:Cytochrome P450 oxidases
655:Ligand-gated ion channel
493:electron transport chain
151:, or can be secreted as
125:bacterial outer membrane
105:
1916:Lipid raft/microdomains
1721:10.1126/science.1076535
1013:Transmembrane receptors
489:succinate dehydrogenase
1921:Membrane contact sites
1885:Lipid-anchored protein
1867:Membrane glycoproteins
1554:Applied Bioinformatics
1330:, Sixth edition, p.546
1328:Molecular Cell Biology
1211:10.1186/1741-7007-7-50
828:Autotransporter domain
815:Lipid A deacylase PagL
663:acetylcholine receptor
593:transporter AcrB, see
477:cytochrome b6f complex
234:
221:
164:gram-positive bacteria
137:gram-positive bacteria
129:gram-negative bacteria
57:conformational changes
36:
1876:transmembrane protein
820:Opacity family porins
689:Methane monooxygenase
499:Cytochrome c oxidases
242:X-ray crystallography
232:
218:
202:endoplasmic reticulum
198:single-pass molecules
84:transmembrane segment
41:transmembrane protein
22:
1901:Caveolae/Coated pits
1326:Harvey Lodish etc.;
1110:Medical cell biology
1008:Transmembrane domain
854:, known as trimeric
744:Pulmonary surfactant
735:) major coat protein
612:Ammonia transporters
595:multidrug resistance
172:polyproline-II helix
1713:2002Sci...298.1793B
1658:2017PLoSO..1282016M
1296:2019PCCP...2122396K
1290:(40): 22396–22408.
1257:10.1021/bi00450a019
1082:"Membrane Proteins"
746:-associated protein
632:KcsA and KvAP, and
475:(cytochrome bc1 );
266:annular lipid shell
254:tertiary structures
246:electron microscopy
153:pore-forming toxins
1926:Membrane nanotubes
1811:Structures of the
1305:10.1039/c9cp02996f
1141:Jin Xiong (2006).
844:transporter FadL (
750:Monoamine oxidases
630:potassium channels
252:. The most common
235:
222:
170:. A transmembrane
37:
1959:
1958:
1859:Membrane proteins
1251:(24): 9379–9385.
1154:978-0-521-84098-9
1120:978-0-12-370458-0
1088:. Garland Science
1049:10.1021/jz300150v
1003:Membrane topology
787:). They include:
733:filamentous phage
720:nitrite reductase
694:Rhomboid protease
674:Chloride channels
555:secretory pathway
481:nitrate reductase
427:Bacteriorhodopsin
375:bacteriorhodopsin
351:bacteriorhodopsin
289:Protein stability
272:Membrane proteins
184:Membrane topology
96:membrane proteins
73:denaturing agents
1979:
1941:Nuclear envelope
1936:Nodes of Ranvier
1805:
1798:
1791:
1782:
1781:
1776:
1775:
1747:
1741:
1740:
1707:(5599): 1793–6.
1696:
1690:
1689:
1679:
1669:
1637:
1631:
1630:
1620:
1610:
1601:(7): 1607–1621.
1586:
1580:
1579:
1569:
1549:
1543:
1542:
1524:
1504:
1498:
1497:
1495:
1494:
1485:. Archived from
1479:
1473:
1472:
1462:
1430:
1424:
1421:
1415:
1414:
1404:
1372:
1366:
1365:
1337:
1331:
1324:
1318:
1317:
1307:
1275:
1269:
1268:
1240:
1234:
1233:
1223:
1213:
1189:
1183:
1172:
1166:
1165:
1163:
1161:
1138:
1132:
1131:
1129:
1127:
1104:
1098:
1097:
1095:
1093:
1077:
1071:
1070:
1060:
1028:
659:neurotransmitter
628:like, including
609:sodium symporter
607:Neurotransmitter
575:carrier proteins
549:ABC transporters
250:NMR spectroscopy
238:Membrane protein
80:peptide sequence
1987:
1986:
1982:
1981:
1980:
1978:
1977:
1976:
1962:
1961:
1960:
1955:
1889:
1853:
1821:Membrane lipids
1815:
1809:
1779:
1748:
1744:
1697:
1693:
1652:(8): e0182016.
1638:
1634:
1587:
1583:
1567:10.1.1.134.7424
1550:
1546:
1522:10.1.1.332.4023
1505:
1501:
1492:
1490:
1481:
1480:
1476:
1431:
1427:
1422:
1418:
1373:
1369:
1338:
1334:
1325:
1321:
1276:
1272:
1241:
1237:
1190:
1186:
1173:
1169:
1159:
1157:
1155:
1139:
1135:
1125:
1123:
1121:
1105:
1101:
1091:
1089:
1078:
1074:
1029:
1025:
1021:
999:
962:
780:
713:T cell receptor
708:
685:
622:
568:
528:
515:
468:
423:
418:
412:
395:
367:
322:disulfide bonds
296:
291:
285:Protein folding
283:Main articles:
281:
227:
186:
180:
141:outer membranes
113:
108:
88:hydropathy plot
17:
12:
11:
5:
1985:
1975:
1974:
1957:
1956:
1954:
1953:
1948:
1946:Phycobilisomes
1943:
1938:
1933:
1928:
1923:
1918:
1913:
1908:
1906:Cell junctions
1903:
1897:
1895:
1891:
1890:
1888:
1887:
1878:
1869:
1863:
1861:
1855:
1854:
1852:
1851:
1846:
1841:
1836:
1831:
1825:
1823:
1817:
1816:
1808:
1807:
1800:
1793:
1785:
1778:
1777:
1758:(5): 1369–81.
1742:
1691:
1632:
1581:
1544:
1515:(1): 125–140.
1499:
1474:
1445:(5): 581–586.
1425:
1416:
1387:(2): 117–125.
1367:
1332:
1319:
1270:
1235:
1184:
1167:
1153:
1133:
1119:
1099:
1072:
1043:(7): 939–944.
1022:
1020:
1017:
1016:
1015:
1010:
1005:
998:
995:
994:
993:
979:
973:
961:
958:
943:
942:
937:porin family (
932:
915:
897:
887:
877:
863:
849:
835:
825:
824:
823:
817:
812:
806:
800:
794:
779:
776:
775:
774:
769:
763:
758:
753:
747:
741:
736:
729:
723:
716:
707:
704:
703:
702:
699:Disulfide bond
696:
691:
684:
681:
680:
679:
676:
671:
666:
652:
647:
642:
637:
621:
618:
617:
616:
613:
610:
604:
601:
598:
584:
577:
567:
564:
563:
562:
551:
546:
536:
533:calcium ATPase
527:
524:
523:
522:
514:
511:
510:
509:
496:
467:
464:
463:
462:
449:
438:
422:
419:
411:
408:
394:
391:
366:
363:
335:unfolded state
330:unfolded state
318:molten globule
295:
292:
280:
277:
226:
223:
210:cell membranes
182:Main article:
179:
176:
112:
109:
107:
104:
15:
9:
6:
4:
3:
2:
1984:
1973:
1970:
1969:
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1931:Myelin sheath
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1845:
1844:Sphingolipids
1842:
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1837:
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1834:Phospholipids
1832:
1830:
1829:Lipid bilayer
1827:
1826:
1824:
1822:
1818:
1814:
1813:cell membrane
1806:
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1489:on 2013-12-25
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718:Cytochrome c
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572:Mitochondrial
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541:
540:phospholamban
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410:3D structures
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302:alpha-helical
300:
299:Transmembrane
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194:lipid bilayer
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117:alpha-helical
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50:
49:cell membrane
46:
43:is a type of
42:
34:
30:
26:
21:
1875:
1839:Lipoproteins
1755:
1752:J. Mol. Biol
1751:
1745:
1704:
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1649:
1645:
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1598:
1594:
1584:
1560:(1): 21–35.
1557:
1553:
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1512:
1508:
1502:
1491:. Retrieved
1487:the original
1477:
1442:
1438:
1428:
1419:
1384:
1380:
1370:
1348:(3): 87–93.
1345:
1342:FEBS Letters
1341:
1335:
1327:
1322:
1287:
1283:
1273:
1248:
1245:Biochemistry
1244:
1238:
1201:
1197:
1187:
1182:, and others
1180:lipoproteins
1178:and certain
1170:
1158:. Retrieved
1143:
1136:
1124:. Retrieved
1109:
1102:
1090:. Retrieved
1085:
1075:
1040:
1036:
1026:
989:
985:
969:
950:
946:
944:
938:
921:
907:
893:
883:
873:
859:
845:
840:, including
831:
784:
711:Subunits of
507:mitochondria
460:chloroplasts
446:photosystems
399:
396:
386:
378:
370:
368:
343:denaturation
334:
328:
326:
313:
306:denaturation
297:
270:
258:helix bundle
236:
225:3D structure
187:
160:gramicidin A
157:
149:chloroplasts
145:mitochondria
121:beta barrels
114:
77:
69:beta-barrels
40:
38:
1160:13 November
1126:24 November
955:beta-barrel
904:plug domain
868:, or sugar
726:Glycophorin
661:receptors (
589:(multidrug
359:amphiphilic
262:beta barrel
98:are called
61:hydrophobic
1911:Glycocalyx
1493:2016-05-01
1092:31 October
1019:References
984:(octamer,
982:MspA porin
902:and their
866:Maltoporin
842:Fatty acid
731:Inovirus (
669:Aquaporins
559:translocon
544:sarcolipin
440:Bacterial
433:(see also
414:See also:
404:chaperones
383:translocon
168:antibiotic
133:cell walls
65:detergents
1951:Porosomes
1562:CiteSeerX
1517:CiteSeerX
970:n=12,S=12
939:n=14,S=16
928:OmpT and
922:n=10,S=12
912:cobalamin
908:n=22,S=24
894:n=12,S=16
884:n=12,S=16
874:n=18,S=22
860:n=16,S=20
846:n=14,S=14
832:n=12,S=14
785:n=8, S=10
431:rhodopsin
347:detergent
100:monotopic
1966:Category
1737:22656813
1729:12459591
1686:28771529
1646:PLOS ONE
1627:22579045
1576:15130854
1539:17579561
1469:18674618
1411:20724162
1362:11532438
1314:31577299
1230:19678920
1198:BMC Biol
1067:22563521
997:See also
926:protease
920:family (
581:permease
553:General
503:bacteria
456:bacteria
448:I and II
387:in vitro
371:in vitro
339:micelles
1849:Sterols
1772:8126726
1709:Bibcode
1701:Science
1677:5542473
1654:Bibcode
1618:3641781
1460:2580798
1402:3161620
1292:Bibcode
1265:2482072
1221:2739160
1176:Stannin
1058:3341589
752:A and B
728:A dimer
722:complex
715:complex
683:Enzymes
531:P-type
520:ATPases
400:in vivo
379:In vivo
314:misfold
310:H-bonds
192:of the
33:β-sheet
29:α-helix
1770:
1735:
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1228:
1218:
1204:: 50.
1151:
1117:
1065:
1055:
990:n=S=14
986:n=S=16
945:Note:
870:porins
856:porins
822:(NspA)
811:(PagP)
805:(OmpW)
799:(OmpX)
793:(OmpA)
636:Kirbac
591:efflux
557:(Sec)
491:. See
333:. The
166:as an
1894:Other
1733:S2CID
739:Pilin
501:from
454:from
435:opsin
206:lumen
204:(ER)
106:Types
1768:PMID
1725:PMID
1682:PMID
1623:PMID
1595:Cell
1572:PMID
1535:PMID
1465:PMID
1407:PMID
1358:PMID
1310:PMID
1261:PMID
1226:PMID
1162:2010
1149:ISBN
1128:2010
1115:ISBN
1094:2023
1063:PMID
949:and
542:and
505:and
458:and
444:and
287:and
260:and
147:and
119:and
78:The
1760:doi
1756:236
1717:doi
1705:298
1672:PMC
1662:doi
1613:PMC
1603:doi
1599:149
1527:doi
1455:PMC
1447:doi
1397:PMC
1389:doi
1350:doi
1346:504
1300:doi
1253:doi
1216:PMC
1206:doi
1053:PMC
1045:doi
657:of
355:SDS
353:in
248:or
143:of
135:of
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Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
