241:
223:). 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.
227:
400:), 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.
286:
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.
417:, 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.
285:
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
230:
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
31:
396:. 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
408:
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
819:
138:. 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
1254:
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".
597:
650:
368:
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
807:
1710:
Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF (November 2002). "Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling".
372:
structures. Free energy differences between such detergent-denatured and native states are similar to stabilities of water-soluble proteins (< 10 kcal/mol).
166:. All beta-barrel transmembrane proteins have simplest up-and-down topology, which may reflect their common evolutionary origin and similar folding mechanism.
848:
211:. 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
925:
transporter BtuB, Fe(III)-pyochelin receptor FptA, receptor FepA, ferric hydroxamate uptake receptor FhuA, transporter FecA, and pyoverdine receptor FpvA
1813:
976:
1761:
Murzin AG, Lesk AM, Chothia C (March 1994). "Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis".
185:
has not been reported in natural proteins. Nonetheless, this structure was experimentally observed in specifically designed artificial peptides.
1205:"Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin"
134:. Alpha-helical proteins are present in the inner membranes of bacterial cells or the plasma membrane of eukaryotic cells, and sometimes in the
644:
1651:
Michalik, Marcin; Orwick-Rydmark, Marcella; Habeck, Michael; Alva, Vikram; Arnold, Thomas; Linke, Dirk; Permyakov, Eugene A. (3 August 2017).
231:
defining transmembrane protein groups, rather location of topogenic determinants and mechanism of assembly is considered in the classification
1163:
1129:
319:
studies, because they do not unfold completely within the membranes (the complete unfolding would require breaking down too many α-helical
1982:
483:
426:
1434:
White, Stephen. "General
Principle of Membrane Protein Folding and Stability". Stephen White Laboratory Homepage. 10 Nov. 2009. web.
689:
Outer membrane auxiliary proteins (polysaccharide transporter) - α-helical transmembrane proteins from the outer bacterial membrane
495:
356:
experiments. This state represents a combination of folded hydrophobic α-helices and partially unfolded segments covered by the
240:
900:
813:
986:
862:
801:
452:
1806:
655:
151:
102:
35:
1891:
940:
928:
353:
316:
169:
In addition to the protein domains, there are unusual transmembrane elements formed by peptides. A typical example is
83:
626:
Drug/Metabolite
Transporter (small multidrug resistance transporter EmrE - the structures are retracted as erroneous)
1493:
766:
264:
110:
63:
1600:
Hopf, Thomas A.; Colwell, Lucy J.; Sheridan, Robert; Rost, Burkhard; Sander, Chris; Marks, Debora S. (June 2012).
1882:
890:
636:
90:
55:
945:
914:
910:
782:
665:
503:
462:
135:
1351:
Goder, Veit; Spiess, Martin (31 August 2001). "Topogenesis of membrane proteins: determinants and dynamics".
1799:
989:, also known as trimeric outer membrane factors (n=12,S=18) including TolC and multidrug resistance proteins
771:
499:
384:
is technically difficult. There are relatively few examples of the successful refolding experiments, as for
1518:
Elofsson, Arne; Heijne, Gunnar von (7 June 2007). "Membrane
Protein Structure: Prediction versus Reality".
1895:
1877:
1572:
1527:
1023:
838:
825:
673:
660:
487:
365:
178:
174:
147:
139:
1931:
830:
699:
601:
252:
226:
212:
1091:
Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter (2002).
1719:
1664:
1302:
1018:
754:
605:
509:
309:
94:
1653:"An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins"
1577:
1532:
414:
276:
256:
1743:
163:
101:. Depending on the number of transmembrane segments, transmembrane proteins can be classified as
113:, meaning that they are also permanently attached to the membrane, but do not pass through it.
1936:
1778:
1735:
1692:
1633:
1582:
1545:
1475:
1417:
1368:
1320:
1271:
1236:
1159:
1153:
1125:
1073:
1013:
776:
760:
743:
730:
704:
640:
565:
491:
437:
385:
361:
299:
194:
182:
1563:
Chen, Chien Peter; Rost, Burkhard (2002). "State-of-the-art in membrane protein prediction".
1541:
1119:
1951:
1869:
1770:
1727:
1682:
1672:
1623:
1613:
1537:
1465:
1457:
1444:
Carpenter, Elisabeth P; Beis, Konstantinos; Cameron, Alexander D; Iwata, So (October 2008).
1407:
1399:
1360:
1310:
1291:"Bilayer thickness determines the alignment of model polyproline helices in lipid membranes"
1263:
1226:
1216:
1063:
1055:
684:
669:
617:
282:
260:
248:
200:
106:
67:
30:
1946:
880:
866:
723:
585:
559:
392:, all such proteins are normally folded co-translationally within the large transmembrane
332:
295:
216:
208:
98:
17:
1723:
1668:
1306:
335:, or unfolding of peripheral regions and nonregular loops that are locally less stable.
1831:
1687:
1652:
1628:
1601:
1470:
1445:
1412:
1387:
1231:
1204:
1068:
1043:
709:
543:
340:
328:
220:
1364:
1976:
1956:
1916:
1839:
1823:
1774:
582:
550:
204:
59:
1747:
173:, a peptide that forms a dimeric transmembrane β-helix. This peptide is secreted by
1854:
1844:
1190:
517:
470:
275:. The portion of the membrane proteins that are attached to the lipid bilayer (see
268:
170:
159:
155:
1791:
1289:
Kubyshkin, Vladimir; Grage, Stephan L.; Ulrich, Anne S.; Budisa, Nediljko (2019).
1677:
1849:
965:
736:
456:
369:
312:
272:
131:
127:
79:
71:
66:
of specific substances across the membrane. They frequently undergo significant
39:
1618:
1403:
1092:
1926:
1921:
1461:
992:
876:
852:
569:
554:
393:
219:
during synthesis (and the extracellular space, if mature forms are located on
43:
1731:
1044:"Environment Polarity in Proteins Mapped Noninvasively by FTIR Spectroscopy"
964:
are, respectively, the number of beta-strands and the "shear number" of the
922:
679:
441:
357:
143:
75:
42:) 2) a multipass membrane protein (α-helix) 3) a multipass membrane protein
1739:
1696:
1637:
1602:"Three-Dimensional Structures of Membrane Proteins from Genomic Sequencing"
1586:
1549:
1479:
1421:
1372:
1324:
1240:
1221:
1077:
1782:
1275:
1961:
1911:
1386:
Cross, Timothy A.; Sharma, Mukesh; Yi, Myunggi; Zhou, Huan-Xiang (2011).
936:
591:
590:
Major
Facilitator Superfamily (Glycerol-3-phosphate transporter, Lactose
513:
466:
349:
1497:
1267:
1388:"Influence of Solubilizing Environments on Membrane Protein Structures"
1315:
1290:
1186:
1059:
611:
Dicarboxylate/amino acid:cation symporter (proton glutamate symporter)
1941:
1859:
820:
Antimicrobial peptide resistance and lipid A acylation protein family
794:
Beta barrels from eight beta-strands and with "shear number" of ten (
614:
Monovalent cation/proton antiporter (Sodium/proton antiporter 1 NhaA)
530:
320:
749:
445:
244:
Increase in the number of 3D structures of membrane proteins known
225:
70:
to move a substance through the membrane. They are usually highly
29:
323:
in the nonpolar media). On the other hand, these proteins easily
327:, due to non-native aggregation in membranes, transition to the
315:(α-helical) proteins are unusually stable judging from thermal
1795:
1446:"Overcoming the challenges of membrane protein crystallography"
201:
position of the protein N- and C-termini on the different sides
1042:
Manor, Joshua; Feldblum, Esther S.; Arkin, Isaiah T. (2012).
78:
or nonpolar solvents for extraction, although some of them (
404:
Stability and folding of beta-barrel transmembrane proteins
1203:
Almén MS, Nordström KJ, Fredriksson R, Schiöth HB (2009).
105:, or as multipass membrane proteins. Some other integral
97:, is largely hydrophobic and can be visualized using the
34:
Schematic representation of transmembrane proteins: 1) a
656:
Small-conductance mechanosensitive ion channel (MscS)
126:
There are two basic types of transmembrane proteins:
74:
and aggregate and precipitate in water. They require
1904:
1868:
1830:
971:
Beta-barrels composed of several polypeptide chains
789:
Beta-barrels composed of a single polypeptide chain
1185:alpha-helical proteins in outer membranes include
917:. They are ligand-gated outer membrane channels (
529:Proton or sodium translocating F-type and V-type
305:Stability of alpha-helical transmembrane proteins
717:Proteins with single transmembrane alpha-helices
651:Large-conductance mechanosensitive channel, MscL
808:Virulence-related outer membrane protein family
380:Refolding of α-helical transmembrane proteins
46:. The membrane is represented in light yellow.
1807:
1158:. Cambridge University Press. pp. 208–.
631:Alpha-helical channels including ion channels
577:Porters (uniporters, symporters, antiporters)
524:Electrochemical potential-driven transporters
279:) consist mostly of hydrophobic amino acids.
27:Protein spanning across a biological membrane
8:
849:FadL outer membrane protein transport family
338:It is also important to properly define the
376:Folding of α-helical transmembrane proteins
1814:
1800:
1792:
1097:Molecular Biology of the Cell. 4th edition
482:Transmembrane cytochrome b-like proteins:
62:. Many transmembrane proteins function as
1686:
1676:
1627:
1617:
1576:
1531:
1494:"Membrane Proteins of known 3D Structure"
1469:
1411:
1314:
1230:
1220:
1067:
1048:The Journal of Physical Chemistry Letters
1542:10.1146/annurev.biochem.76.052705.163539
239:
1034:
537:P-P-bond hydrolysis-driven transporters
645:inward-rectifier potassium ion channel
352:is different from that in the thermal
1450:Current Opinion in Structural Biology
712:formation protein (DsbA-DsbB complex)
490:; formate dehydrogenase, respiratory
7:
432:Light absorption-driven transporters
267:of these proteins are transmembrane
1295:Physical Chemistry Chemical Physics
598:Resistance-nodulation-cell division
484:coenzyme Q - cytochrome c reductase
427:Transporter Classification Database
290:Thermodynamic stability and folding
477:Oxidoreduction-driven transporters
348:of membrane proteins in detergent
199:This classification refers to the
25:
777:Corticosteroid 11β-dehydrogenases
594:, and Multidrug transporter EmrD)
1124:. Academic Press. pp. 37–.
1003:) . These proteins are secreted.
496:succinate - coenzyme Q reductase
413:is facilitated by water-soluble
331:states, formation of non-native
251:structures can be determined by
93:that spans the membrane, or the
64:gateways to permit the transport
935:) that includes outer membrane
901:Outer membrane phospholipase A1
814:Outer membrane protein W family
453:photosynthetic reaction centres
58:that spans the entirety of the
1392:Trends in Biochemical Sciences
987:Outer membrane efflux proteins
863:General bacterial porin family
802:OmpA-like transmembrane domain
546:(five different conformations)
360:. For example, the "unfolded"
207:. Types I, II, III and IV are
82:) can be also extracted using
1:
1520:Annual Review of Biochemistry
1365:10.1016/S0014-5793(01)02712-0
572:(preprotein translocase SecY)
103:single-pass membrane proteins
1775:10.1016/0022-2836(94)90064-7
1678:10.1371/journal.pone.0182016
999:) and α-hemolysin (heptamer
941:adhesin/invasin OpcA protein
36:single-pass membrane protein
1892:Peripheral membrane protein
929:Outer membrane protein OpcA
661:CorA metal ion transporters
122:Classification by structure
1999:
1983:Integral membrane proteins
1883:Integral membrane proteins
1619:10.1016/j.cell.2012.04.012
1404:10.1016/j.tibs.2010.07.005
1118:Steven R. Goodman (2008).
767:Fatty acid amide hydrolase
549:Calcium ATPase regulators
498:(fumarate reductase); and
463:Light-harvesting complexes
424:
293:
192:
189:Classification by topology
18:Integral polytopic protein
1462:10.1016/j.sbi.2008.07.001
891:Nucleoside-specific porin
637:Voltage-gated ion channel
440:-like proteins including
56:integral membrane protein
1155:Essential bioinformatics
977:Trimeric autotransporter
946:Outer membrane protein G
911:TonB-dependent receptors
783:Signal Peptide Peptidase
772:Cytochrome P450 oxidases
666:Ligand-gated ion channel
504:electron transport chain
162:, or can be secreted as
136:bacterial outer membrane
1927:Lipid raft/microdomains
1732:10.1126/science.1076535
1024:Transmembrane receptors
500:succinate dehydrogenase
1932:Membrane contact sites
1896:Lipid-anchored protein
1878:Membrane glycoproteins
1565:Applied Bioinformatics
1341:, Sixth edition, p.546
1339:Molecular Cell Biology
1222:10.1186/1741-7007-7-50
839:Autotransporter domain
826:Lipid A deacylase PagL
674:acetylcholine receptor
604:transporter AcrB, see
488:cytochrome b6f complex
245:
232:
175:gram-positive bacteria
148:gram-positive bacteria
140:gram-negative bacteria
68:conformational changes
47:
1887:transmembrane protein
831:Opacity family porins
700:Methane monooxygenase
510:Cytochrome c oxidases
253:X-ray crystallography
243:
229:
213:endoplasmic reticulum
209:single-pass molecules
95:transmembrane segment
52:transmembrane protein
33:
1912:Caveolae/Coated pits
1337:Harvey Lodish etc.;
1121:Medical cell biology
1019:Transmembrane domain
865:, known as trimeric
755:Pulmonary surfactant
746:) major coat protein
623:Ammonia transporters
606:multidrug resistance
183:polyproline-II helix
1724:2002Sci...298.1793B
1669:2017PLoSO..1282016M
1307:2019PCCP...2122396K
1301:(40): 22396–22408.
1268:10.1021/bi00450a019
1093:"Membrane Proteins"
757:-associated protein
643:KcsA and KvAP, and
486:(cytochrome bc1 );
277:annular lipid shell
265:tertiary structures
257:electron microscopy
164:pore-forming toxins
1937:Membrane nanotubes
1822:Structures of the
1316:10.1039/c9cp02996f
1152:Jin Xiong (2006).
855:transporter FadL (
761:Monoamine oxidases
641:potassium channels
263:. The most common
246:
233:
181:. A transmembrane
48:
1970:
1969:
1870:Membrane proteins
1262:(24): 9379–9385.
1165:978-0-521-84098-9
1131:978-0-12-370458-0
1099:. Garland Science
1060:10.1021/jz300150v
1014:Membrane topology
798:). They include:
744:filamentous phage
731:nitrite reductase
705:Rhomboid protease
685:Chloride channels
566:secretory pathway
492:nitrate reductase
438:Bacteriorhodopsin
386:bacteriorhodopsin
362:bacteriorhodopsin
300:Protein stability
283:Membrane proteins
195:Membrane topology
107:membrane proteins
84:denaturing agents
16:(Redirected from
1990:
1952:Nuclear envelope
1947:Nodes of Ranvier
1816:
1809:
1802:
1793:
1787:
1786:
1758:
1752:
1751:
1718:(5599): 1793–6.
1707:
1701:
1700:
1690:
1680:
1648:
1642:
1641:
1631:
1621:
1612:(7): 1607–1621.
1597:
1591:
1590:
1580:
1560:
1554:
1553:
1535:
1515:
1509:
1508:
1506:
1505:
1496:. Archived from
1490:
1484:
1483:
1473:
1441:
1435:
1432:
1426:
1425:
1415:
1383:
1377:
1376:
1348:
1342:
1335:
1329:
1328:
1318:
1286:
1280:
1279:
1251:
1245:
1244:
1234:
1224:
1200:
1194:
1183:
1177:
1176:
1174:
1172:
1149:
1143:
1142:
1140:
1138:
1115:
1109:
1108:
1106:
1104:
1088:
1082:
1081:
1071:
1039:
670:neurotransmitter
639:like, including
620:sodium symporter
618:Neurotransmitter
586:carrier proteins
560:ABC transporters
261:NMR spectroscopy
249:Membrane protein
91:peptide sequence
21:
1998:
1997:
1993:
1992:
1991:
1989:
1988:
1987:
1973:
1972:
1971:
1966:
1900:
1864:
1832:Membrane lipids
1826:
1820:
1790:
1760:
1759:
1755:
1709:
1708:
1704:
1663:(8): e0182016.
1650:
1649:
1645:
1599:
1598:
1594:
1578:10.1.1.134.7424
1562:
1561:
1557:
1533:10.1.1.332.4023
1517:
1516:
1512:
1503:
1501:
1492:
1491:
1487:
1443:
1442:
1438:
1433:
1429:
1385:
1384:
1380:
1350:
1349:
1345:
1336:
1332:
1288:
1287:
1283:
1253:
1252:
1248:
1202:
1201:
1197:
1184:
1180:
1170:
1168:
1166:
1151:
1150:
1146:
1136:
1134:
1132:
1117:
1116:
1112:
1102:
1100:
1090:
1089:
1085:
1041:
1040:
1036:
1032:
1010:
973:
791:
724:T cell receptor
719:
696:
633:
579:
539:
526:
479:
434:
429:
423:
406:
378:
333:disulfide bonds
307:
302:
296:Protein folding
294:Main articles:
292:
238:
197:
191:
152:outer membranes
124:
119:
99:hydropathy plot
28:
23:
22:
15:
12:
11:
5:
1996:
1994:
1986:
1985:
1975:
1974:
1968:
1967:
1965:
1964:
1959:
1957:Phycobilisomes
1954:
1949:
1944:
1939:
1934:
1929:
1924:
1919:
1917:Cell junctions
1914:
1908:
1906:
1902:
1901:
1899:
1898:
1889:
1880:
1874:
1872:
1866:
1865:
1863:
1862:
1857:
1852:
1847:
1842:
1836:
1834:
1828:
1827:
1821:
1819:
1818:
1811:
1804:
1796:
1789:
1788:
1769:(5): 1369–81.
1753:
1702:
1643:
1592:
1555:
1526:(1): 125–140.
1510:
1485:
1456:(5): 581–586.
1436:
1427:
1398:(2): 117–125.
1378:
1343:
1330:
1281:
1246:
1195:
1178:
1164:
1144:
1130:
1110:
1083:
1054:(7): 939–944.
1033:
1031:
1028:
1027:
1026:
1021:
1016:
1009:
1006:
1005:
1004:
990:
984:
972:
969:
954:
953:
948:porin family (
943:
926:
908:
898:
888:
874:
860:
846:
836:
835:
834:
828:
823:
817:
811:
805:
790:
787:
786:
785:
780:
774:
769:
764:
758:
752:
747:
740:
734:
727:
718:
715:
714:
713:
710:Disulfide bond
707:
702:
695:
692:
691:
690:
687:
682:
677:
663:
658:
653:
648:
632:
629:
628:
627:
624:
621:
615:
612:
609:
595:
588:
578:
575:
574:
573:
562:
557:
547:
544:calcium ATPase
538:
535:
534:
533:
525:
522:
521:
520:
507:
478:
475:
474:
473:
460:
449:
433:
430:
422:
419:
405:
402:
377:
374:
346:unfolded state
341:unfolded state
329:molten globule
306:
303:
291:
288:
237:
234:
221:cell membranes
193:Main article:
190:
187:
123:
120:
118:
115:
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
1995:
1984:
1981:
1980:
1978:
1963:
1960:
1958:
1955:
1953:
1950:
1948:
1945:
1943:
1942:Myelin sheath
1940:
1938:
1935:
1933:
1930:
1928:
1925:
1923:
1920:
1918:
1915:
1913:
1910:
1909:
1907:
1903:
1897:
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1855:Sphingolipids
1853:
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1845:Phospholipids
1843:
1841:
1840:Lipid bilayer
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1833:
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1824:cell membrane
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1500:on 2013-12-25
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729:Cytochrome c
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583:Mitochondrial
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551:phospholamban
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421:3D structures
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313:alpha-helical
311:
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60:cell membrane
57:
54:is a type of
53:
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1886:
1850:Lipoproteins
1766:
1763:J. Mol. Biol
1762:
1756:
1715:
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1660:
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1571:(1): 21–35.
1568:
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1502:. Retrieved
1498:the original
1488:
1453:
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1381:
1359:(3): 87–93.
1356:
1353:FEBS Letters
1352:
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1338:
1333:
1298:
1294:
1284:
1259:
1256:Biochemistry
1255:
1249:
1212:
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1198:
1193:, and others
1191:lipoproteins
1189:and certain
1181:
1169:. Retrieved
1154:
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1135:. Retrieved
1120:
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1101:. Retrieved
1096:
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1000:
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980:
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957:
955:
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904:
894:
884:
870:
856:
851:, including
842:
795:
722:Subunits of
518:mitochondria
471:chloroplasts
457:photosystems
410:
407:
397:
389:
381:
379:
354:denaturation
345:
339:
337:
324:
317:denaturation
308:
281:
269:helix bundle
247:
236:3D structure
198:
171:gramicidin A
168:
160:chloroplasts
156:mitochondria
132:beta barrels
125:
88:
80:beta-barrels
51:
49:
1171:13 November
1137:24 November
966:beta-barrel
915:plug domain
879:, or sugar
737:Glycophorin
672:receptors (
600:(multidrug
370:amphiphilic
273:beta barrel
109:are called
72:hydrophobic
1922:Glycocalyx
1504:2016-05-01
1103:31 October
1030:References
995:(octamer,
993:MspA porin
913:and their
877:Maltoporin
853:Fatty acid
742:Inovirus (
680:Aquaporins
570:translocon
555:sarcolipin
451:Bacterial
444:(see also
425:See also:
415:chaperones
394:translocon
179:antibiotic
144:cell walls
76:detergents
1962:Porosomes
1573:CiteSeerX
1528:CiteSeerX
981:n=12,S=12
950:n=14,S=16
939:OmpT and
933:n=10,S=12
923:cobalamin
919:n=22,S=24
905:n=12,S=16
895:n=12,S=16
885:n=18,S=22
871:n=16,S=20
857:n=14,S=14
843:n=12,S=14
796:n=8, S=10
442:rhodopsin
358:detergent
111:monotopic
1977:Category
1748:22656813
1740:12459591
1697:28771529
1657:PLOS ONE
1638:22579045
1587:15130854
1550:17579561
1480:18674618
1422:20724162
1373:11532438
1325:31577299
1241:19678920
1209:BMC Biol
1078:22563521
1008:See also
937:protease
931:family (
592:permease
564:General
514:bacteria
467:bacteria
459:I and II
398:in vitro
382:in vitro
350:micelles
1860:Sterols
1783:8126726
1720:Bibcode
1712:Science
1688:5542473
1665:Bibcode
1629:3641781
1471:2580798
1413:3161620
1303:Bibcode
1276:2482072
1232:2739160
1187:Stannin
1069:3341589
763:A and B
739:A dimer
733:complex
726:complex
694:Enzymes
542:P-type
531:ATPases
411:in vivo
390:In vivo
325:misfold
321:H-bonds
203:of the
44:β-sheet
40:α-helix
1781:
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1229:
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1001:n=S=14
997:n=S=16
956:Note:
881:porins
867:porins
833:(NspA)
822:(PagP)
816:(OmpW)
810:(OmpX)
804:(OmpA)
647:Kirbac
602:efflux
568:(Sec)
502:. See
344:. The
177:as an
1905:Other
1744:S2CID
750:Pilin
512:from
465:from
446:opsin
217:lumen
215:(ER)
117:Types
1779:PMID
1736:PMID
1693:PMID
1634:PMID
1606:Cell
1583:PMID
1546:PMID
1476:PMID
1418:PMID
1369:PMID
1321:PMID
1272:PMID
1237:PMID
1173:2010
1160:ISBN
1139:2010
1126:ISBN
1105:2023
1074:PMID
960:and
553:and
516:and
469:and
455:and
298:and
271:and
158:and
130:and
89:The
1771:doi
1767:236
1728:doi
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1683:PMC
1673:doi
1624:PMC
1614:doi
1610:149
1538:doi
1466:PMC
1458:doi
1408:PMC
1400:doi
1361:doi
1357:504
1311:doi
1264:doi
1227:PMC
1217:doi
1064:PMC
1056:doi
668:of
366:SDS
364:in
259:or
154:of
146:of
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