502:) are about (–120°, 115°) in parallel sheets. It is rare to find less than five interacting parallel strands in a motif, suggesting that a smaller number of strands may be unstable, however it is also fundamentally more difficult for parallel β-sheets to form because strands with N and C termini aligned necessarily must be very distant in sequence . There is also evidence that parallel β-sheet may be more stable since small amyloidogenic sequences appear to generally aggregate into β-sheet fibrils composed of primarily parallel β-sheet strands, where one would expect anti-parallel fibrils if anti-parallel were more stable.
42:
354:
393:
664:
290:
159:
1004:
52:
963:
790:
Protein A (OspA) variants and the Single Layer β-sheet
Proteins (SLBPs) which contain single-layer β-sheets in the absence of a traditional hydrophobic core. These β-rich proteins feature an extended single-layer β-meander β-sheets that are primarily stabilized via inter-β-strand interactions and hydrophobic interactions present in the turn regions connecting individual strands.
566:
arrangement, however bioinformatic analysis always struggles with extracting structural thermodynamics since there are always numerous other structural features present in whole proteins. Also proteins are inherently constrained by folding kinetics as well as folding thermodynamics, so one must always be careful in concluding stability from bioinformatic analysis.
652:
565:
Finally, an individual strand may exhibit a mixed bonding pattern, with a parallel strand on one side and an antiparallel strand on the other. Such arrangements are less common than a random distribution of orientations would suggest, suggesting that this pattern is less stable than the anti-parallel
447:
In an antiparallel arrangement, the successive β-strands alternate directions so that the N-terminus of one strand is adjacent to the C-terminus of the next. This is the arrangement that produces the strongest inter-strand stability because it allows the inter-strand hydrogen bonds between carbonyls
241:
groups in the backbone of the adjacent strands. In the fully extended β-strand, successive side chains point straight up and straight down in an alternating pattern. Adjacent β-strands in a β-sheet are aligned so that their C atoms are adjacent and their side chains point in the same direction. The
1054:
The side chains from the amino acid residues found in a β-sheet structure may also be arranged such that many of the adjacent sidechains on one side of the sheet are hydrophobic, while many of those adjacent to each other on the alternate side of the sheet are polar or charged (hydrophilic), which
798:
The psi-loop (Ψ-loop) motif consists of two antiparallel strands with one strand in between that is connected to both by hydrogen bonds. There are four possible strand topologies for single Ψ-loops. This motif is rare as the process resulting in its formation seems unlikely to occur during protein
749:
The β-meander motif from Outer surface protein A (OspA). The image above shows a variant of OspA (OspA+3bh) that contains a central, extended β-meander β-sheet featuring three additional copies (in red) of the core OspA β-hairpin (in grey) that have been duplicated and reinserted into the parent
729:
Due to the chirality of their component amino acids, all strands exhibit right-handed twist evident in most higher-order β-sheet structures. In particular, the linking loop between two parallel strands almost always has a right-handed crossover chirality, which is strongly favored by the inherent
174:
file 1GWE at 0.88 Å resolution). a) Front view, showing the antiparallel hydrogen bonds (dotted) between peptide NH and CO groups on adjacent strands. Arrows indicate chain direction, and electron density contours outline the non-hydrogen atoms. Oxygen atoms are red balls, nitrogen atoms are
867:
has a five-stranded, parallel β-sheet with topology 21345; thus, the edge strands are β-strand 2 and β-strand 5 along the backbone. Spelled out explicitly, β-strand 2 is H-bonded to β-strand 1, which is H-bonded to β-strand 3, which is H-bonded to β-strand 4, which is H-bonded to β-strand 5, the
789:
The vast majority of β-meander regions in proteins are found packed against other motifs or sections of the polypeptide chain, forming portions of the hydrophobic core that canonically drives formation of the folded structure. However, several notable exceptions include the Outer
Surface
712:
The Greek key motif consists of four adjacent antiparallel strands and their linking loops. It consists of three antiparallel strands connected by hairpins, while the fourth is adjacent to the first and linked to the third by a longer loop. This type of structure forms easily during the
242:"pleated" appearance of β-strands arises from tetrahedral chemical bonding at the C atom; for example, if a side chain points straight up, then the bonds to the C′ must point slightly downwards, since its bond angle is approximately 109.5°. The pleating causes the distance between C
984:
is formed from repeating structural units consisting of two or three short β-strands linked by short loops. These units "stack" atop one another in a helical fashion so that successive repetitions of the same strand hydrogen-bond with each other in a parallel orientation. See the
31:
1035:; its two loops are each six residues long and bind stabilizing calcium ions to maintain the integrity of the structure, using the backbone and the Asp side chain oxygens of a GGXGXD sequence motif. This fold is called a β-roll in the SCOP classification.
493:
In a parallel arrangement, all of the N-termini of successive strands are oriented in the same direction; this orientation may be slightly less stable because it introduces nonplanarity in the inter-strand hydrogen bonding pattern. The dihedral angles
746:
1029:, have a less regular cross-section, longer and indented on one of the sides; of the three linker loops, one is consistently just two residues long and the others are variable, often elaborated to form a binding or active site.
755:
195:
of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids in order to build accurate models, especially since he did not then know that the
1483:
Xu, Qingping; Biancalana, Matthew; Grant, Joanna C.; Chiu, Hsiu-Ju; Jaroszewski, Lukasz; Knuth, Mark W.; Lesley, Scott A.; Godzik, Adam; Elsliger, Marc-André; Deacon, Ashley M.; Wilson, Ian A. (September 2019).
175:
blue, and hydrogen atoms are omitted for simplicity; sidechains are shown only out to the first sidechain carbon atom (green). b) Edge-on view of the central two β-strands in a, showing the righthanded
340:
The side chains point outwards from the folds of the pleats, roughly perpendicularly to the plane of the sheet; successive amino acid residues point outwards on alternating faces of the sheet.
2166:
440:, β-strands too can be said to be directional. They are usually represented in protein topology diagrams by an arrow pointing toward the C-terminus. Adjacent β-strands can form
45:
301:) plot of about 100,000 high-resolution data points, showing the broad, favorable region around the conformation typical for β-sheet amino acid residues.
1047:) can form β-sheet-rich oligomeric structures associated with pathological states. The amyloid β protein's oligomeric form is implicated as a cause of
2159:
1904:"Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif"
535:
hydrogen bond to each other; rather, one residue forms hydrogen bonds to the residues that flank the other (but not vice versa). For example, residue
333:
to prevent the individual β-strands in a larger sheet from splaying apart. A good example of a strongly twisted β-hairpin can be seen in the protein
992:
In lefthanded β-helices, the strands themselves are quite straight and untwisted; the resulting helical surfaces are nearly flat, forming a regular
1826:
Liou YC, Tocilj A, Davies PL, Jia Z (July 2000). "Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein".
2072:
1399:
2152:
947:
2096:
1374:
2314:
1886:
1268:
1125:
208:
in 1951. Their model incorporated the planarity of the peptide bond which they previously explained as resulting from keto-enol
2130:
1687:"SCOPe: Structural Classification of Proteins--extended, integrating SCOP and ASTRAL data and classification of new structures"
1051:. Its structure has yet to be determined in full, but recent data suggest that it may resemble an unusual two-strand β-helix.
639:
strands in β-sheets, presumably to avoid the "edge-to-edge" association between proteins that might lead to aggregation and
938:β-pleated sheet structures are made from extended β-strand polypeptide chains, with strands linked to their neighbours by
2181:
1026:
734:
motif. A closely related motif called a β-α-β-α motif forms the basic component of the most commonly observed protein
587:
groups pointing in alternating directions with successive residues; for comparison, successive carbonyls point in the
163:
100:
66:
684:, in which two antiparallel strands are linked by a short loop of two to five residues, of which one is frequently a
1000:
and insect antifreeze proteins with a regular array of Thr sidechains on one face that mimic the structure of ice.
996:
shape, as shown for the 1QRE archaeal carbonic anhydrase at right. Other examples are the lipid A synthesis enzyme
1593:
Hutchinson EG, Thornton JM (1990). "HERA--a program to draw schematic diagrams of protein secondary structures".
35:
127:
47:
305:
However, β-strands are rarely perfectly extended; rather, they exhibit a twist. The energetically preferred
353:
46:
1048:
919:
800:
143:
1215:
Hutchinson EG, Thornton JM (April 1993). "The Greek key motif: extraction, classification and analysis".
872:
of a β-sheet can be described roughly by giving the number of strands, their topology, and whether their
730:
twist of the sheet. This linking loop frequently contains a helical region, in which case it is called a
1055:
can be useful if the sheet is to form a boundary between polar/watery and nonpolar/greasy environments.
923:
840:
778:
loops. This motif is common in β-sheets and can be found in several structural architectures including
392:
2021:
1964:
1835:
1782:
1734:
Painter PC, Mosher LE, Rhoads C (July 1982). "Low-frequency modes in the Raman spectra of proteins".
1437:
1328:
1154:
731:
448:
and amines to be planar, which is their preferred orientation. The peptide backbone dihedral angles (
868:
other edge strand. In the same system, the Greek key motif described above has a 4123 topology. The
2246:
1074:
927:
888:
869:
816:
693:
663:
275:
2080:
1403:
700:. Individual strands can also be linked in more elaborate ways with longer loops that may contain
289:
2010:"Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane"
1859:
1618:
1286:
1079:
951:
759:
735:
820:
774:
protein topology composed of two or more consecutive antiparallel β-strands linked together by
2220:
2049:
1990:
1933:
1882:
1851:
1808:
1751:
1716:
1667:
1610:
1572:
1523:
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1465:
1356:
1274:
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1232:
1182:
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1009:
968:
828:
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318:
171:
158:
71:
2289:
2104:
2039:
2029:
1980:
1972:
1923:
1915:
1843:
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1790:
1743:
1706:
1698:
1657:
1649:
1602:
1562:
1554:
1513:
1497:
1455:
1445:
1378:
1346:
1336:
1256:
1224:
1172:
1162:
1117:
1089:
993:
771:
677:
402:
363:
96:
1315:
Makabe K, McElheny D, Tereshko V, Hilyard A, Gawlak G, Yan S, et al. (November 2006).
1003:
329:) = (–180°, 180°). The twist is often associated with alternating fluctuations in the
2134:
1951:
Nelson R, Sawaya MR, Balbirnie M, Madsen AØ, Riekel C, Grothe R, Eisenberg D (June 2005).
1298:
1032:
997:
884:
864:
714:
697:
209:
188:
135:
130:. The supramolecular association of β-sheets has been implicated in the formation of the
2025:
1968:
1839:
1786:
1441:
1332:
1199:
1158:
2225:
1985:
1952:
1919:
1803:
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1711:
1686:
1567:
1542:
1518:
1485:
1460:
1425:
1351:
1316:
1064:
1044:
939:
783:
437:
330:
306:
266:
225:
The majority of β-strands are arranged adjacent to other strands and form an extensive
131:
112:
62:
1928:
1903:
1794:
1662:
1637:
1260:
1177:
1142:
482:β-strands, then they form two mutual backbone hydrogen bonds to each other's flanking
183:
of Cs and sidechains that alternately stick out in opposite directions from the sheet.
2308:
2044:
2009:
1022:
873:
860:
836:
718:
608:
570:
528:
479:
441:
283:
234:
226:
201:
147:
115:
2127:
1622:
2258:
1863:
1143:"Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation"
1110:
775:
681:
656:
581:
483:
456:) are about (–140°, 135°) in antiparallel sheets. In this case, if two atoms C
279:
205:
197:
192:
30:
1204:
Principles of
Protein Structure, Comparative Protein Modelling, and Visualisation
1043:
Some proteins that are disordered or helical as monomers, such as amyloid β (see
692:, both of which can assume the dihedral-angle conformations required for a tight
573:
of β-strands need not be perfect, but can exhibit localized disruptions known as
2284:
2268:
2196:
1084:
903:
894:
832:
779:
701:
592:
139:
2014:
Proceedings of the
National Academy of Sciences of the United States of America
1430:
Proceedings of the
National Academy of Sciences of the United States of America
1321:
Proceedings of the
National Academy of Sciences of the United States of America
1147:
Proceedings of the
National Academy of Sciences of the United States of America
962:
2263:
2215:
2144:
1228:
986:
981:
943:
915:
899:
844:
739:
717:
process. It was named after a pattern common to Greek ornamental artwork (see
624:
612:
574:
559:
433:
273:), rather than the 7.6 Å (0.76 nm) expected from two fully extended
123:
1509:
2251:
2201:
1486:"Structures of single-layer β-sheet proteins evolved from β-hairpin repeats"
1450:
1341:
1069:
914:. Some open β-sheets are very curved and fold over on themselves (as in the
616:
270:
2139:
2034:
1994:
1855:
1720:
1653:
1606:
1558:
1543:"PROMOTIF--a program to identify and analyze structural motifs in proteins"
1527:
1469:
1360:
1186:
1167:
745:
17:
2053:
1937:
1812:
1755:
1747:
1702:
1671:
1614:
1576:
1278:
1236:
651:
558:
The hydrogen bond arrangement in parallel beta sheet resembles that in an
2210:
604:
584:
416:
377:
238:
167:
118:, forming a generally twisted, pleated sheet. A β-strand is a stretch of
1976:
1771:"Low-frequency motions in protein molecules. Beta-sheet and beta-barrel"
1251:
Richardson JS (1981). "The
Anatomy and Taxonomy of Protein Structure".
1203:
824:
689:
685:
640:
632:
555:
may hydrogen-bond to different residues altogether, or to none at all.
119:
75:
1013:
972:
1847:
1501:
620:
406:
367:
754:
580:
The hydrogen bonds lie roughly in the plane of the sheet, with the
191:
in the 1930s. He proposed the idea of hydrogen bonding between the
69:. Cartoon above, atoms below with nitrogen in blue, oxygen in red (
2140:
NetSurfP - Secondary
Structure and Surface Accessibility predictor
1002:
961:
753:
744:
662:
650:
288:
230:
157:
29:
432:
Because peptide chains have a directionality conferred by their
334:
51:
2148:
40:
1031:
A two-sided β-helix (right-handed) is found in some bacterial
942:. Due to this extended backbone conformation, β-sheets resist
321:) diverge significantly from the fully extended conformation (
317:) = (–135°, 135°) (broadly, the upper left region of the
1636:
Hubbard TJ, Murzin AG, Brenner SE, Chothia C (January 1997).
1426:"Minimalist design of water-soluble cross-beta architecture"
827:
or small proteins with poorly defined overall architecture.
50:
1953:"Structure of the cross-beta pine of amyloid-like fibrils"
1902:
Baumann U, Wu S, Flaherty KM, McKay DB (September 1993).
1638:"SCOP: a structural classification of proteins database"
922:). Open β-sheets can assemble face-to-face (such as the
166:β-sheet fragment from a crystal structure of the enzyme
34:
Three-dimensional structure of parts of a beta sheet in
282:. The "sideways" distance between adjacent C atoms in
1200:
Tertiary
Protein Structure and Folds: section 4.3.2.1
883:, meaning that they have two edge strands (as in the
2128:
Anatomy & Taxonomy of Protein Structures -survey
2008:
Zhang S, Holmes T, Lockshin C, Rich A (April 1993).
2277:
2234:
2189:
2180:
1317:"Atomic structures of peptide self-assembly mimics"
2077:Principles of Protein Structure Using the Internet
1109:
807:Structural architectures of proteins with β-sheets
631:of β-sheets. Different types of residues (such as
444:in antiparallel, parallel, or mixed arrangements.
1685:Fox NK, Brenner SE, Chandonia JM (January 2014).
1424:Biancalana M, Makabe K, Koide S (February 2010).
799:folding. The Ψ-loop was first identified in the
863:β-strands along the backbone. For example, the
233:groups in the backbone of one strand establish
111:) connected laterally by at least two or three
44:
1588:
1586:
627:) are favored to be found in β-strands in the
286:β-strands is roughly 5 Å (0.50 nm).
200:was planar. A refined version was proposed by
2160:
1116:(3rd ed.). Hoboken, NJ: Wiley. pp.
1007:End-view of a 3-sided, right-handed β-helix (
954:and analyzed with the quasi-continuum model.
505:In parallel β-sheet structure, if two atoms C
8:
2101:Structural Classification of Proteins (SCOP)
1541:Hutchinson EG, Thornton JM (February 1996).
966:End-view of a 3-sided, left handed β-helix (
930:) or edge-to-edge, forming one big β-sheet.
187:The first β-sheet structure was proposed by
1141:Richardson JS, Richardson DC (March 2002).
2186:
2167:
2153:
2145:
1253:Anatomy and Taxonomy of Protein Structures
229:network with their neighbors in which the
2043:
2033:
1984:
1927:
1802:
1710:
1661:
1566:
1517:
1459:
1449:
1350:
1340:
1176:
1166:
950:accordion-like motion as observed by the
551:of hydrogen bonds. By contrast, residue
55:The image above contains clickable links
1100:
1021:Righthanded β-helices, typified by the
405:patterns, represented by dotted lines.
366:patterns, represented by dotted lines.
1294:
1284:
918:) or form horseshoe shapes (as in the
2073:"Super Secondary Structure - Part II"
1881:. New York: Garland. pp. 20–32.
1400:"PPS '96 – Super Secondary Structure"
946:. β-sheets in proteins may carry out
7:
1310:
1308:
859:of a β-sheet describes the order of
539:may form hydrogen bonds to residues
547: + 1; this is known as a
1920:10.1002/j.1460-2075.1993.tb06009.x
1255:. Vol. 34. pp. 167–339.
1249:See sections II B and III C, D in
126:long with backbone in an extended
25:
2103:. 20 October 2006. Archived from
1879:Introduction to Protein Structure
989:article for further information.
635:) are likely to be found in the
391:
352:
876:are parallel or antiparallel.
615:) and β-branched amino acids (
1:
1795:10.1016/S0006-3495(85)83782-6
1261:10.1016/s0065-3233(08)60520-3
906:are often described by their
1375:"SCOP: Fold: WW domain-like"
2182:Protein secondary structure
2175:Protein secondary structure
1877:Branden C, Tooze J (1999).
1027:P22 phage tailspike protein
265:to be approximately 6
162:An example of a 4-stranded
101:protein secondary structure
67:protein secondary structure
2331:
1697:(Database issue): D304-9.
680:involving β-sheets is the
2315:Protein structural motifs
2097:"Open-sided Beta-meander"
603:Large aromatic residues (
344:Hydrogen bonding patterns
216:Structure and orientation
103:. Beta sheets consist of
36:green fluorescent protein
2071:Cooper J (31 May 1996).
1108:Voet D, Voet JG (2004).
1025:enzyme shown at left or
811:β-sheets are present in
647:Common structural motifs
531:β-strands, then they do
122:chain typically 3 to 10
27:Protein structural motif
1769:Chou KC (August 1985).
1451:10.1073/pnas.0912654107
1342:10.1073/pnas.0606690103
1229:10.1093/protein/6.3.233
599:Amino acid propensities
2035:10.1073/pnas.90.8.3334
1691:Nucleic Acids Research
1642:Nucleic Acids Research
1607:10.1002/prot.340080303
1559:10.1002/pro.5560050204
1168:10.1073/pnas.052706099
1018:
977:
920:ribonuclease inhibitor
762:
751:
668:
660:
302:
184:
80:
56:
38:
1748:10.1002/bip.360210715
1006:
965:
823:domains, and in many
757:
748:
666:
654:
562:motif with 11 atoms.
486:; this is known as a
292:
161:
54:
49:
33:
1654:10.1093/nar/25.1.236
758:Psi-loop motif from
527:are adjacent in two
478:are adjacent in two
2083:on 28 December 2016
2026:1993PNAS...90.3334Z
1977:10.1038/nature03680
1969:2005Natur.435..773N
1840:2000Natur.406..322L
1787:1985BpJ....48..289C
1775:Biophysical Journal
1703:10.1093/nar/gkt1240
1442:2010PNAS..107.3469B
1333:2006PNAS..10317753M
1217:Protein Engineering
1159:2002PNAS...99.2754R
1075:Folding (chemistry)
928:immunoglobulin fold
889:immunoglobulin fold
870:secondary structure
851:Structural topology
667:The Greek-key motif
543: − 1 and
490:of hydrogen bonds.
144:Alzheimer's disease
59:Interactive diagram
2133:2019-03-16 at the
2107:on 4 February 2012
1080:Tertiary structure
1019:
978:
958:Parallel β-helices
952:Raman spectroscopy
924:β-propeller domain
763:
760:Carboxypeptidase A
752:
736:tertiary structure
669:
661:
409:atoms are colored
370:atoms are colored
303:
185:
136:protein aggregates
81:
57:
39:
2302:
2301:
2298:
2297:
2221:Polyproline helix
891:) or they can be
801:aspartic protease
591:direction in the
319:Ramachandran plot
16:(Redirected from
2322:
2290:Helix-turn-helix
2187:
2169:
2162:
2155:
2146:
2116:
2114:
2112:
2092:
2090:
2088:
2079:. Archived from
2058:
2057:
2047:
2037:
2005:
1999:
1998:
1988:
1948:
1942:
1941:
1931:
1908:The EMBO Journal
1899:
1893:
1892:
1874:
1868:
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1848:10.1038/35018604
1823:
1817:
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1714:
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1570:
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1532:
1531:
1521:
1502:10.1002/pro.3683
1496:(9): 1676–1689.
1480:
1474:
1473:
1463:
1453:
1421:
1415:
1414:
1412:
1411:
1402:. Archived from
1396:
1390:
1389:
1387:
1386:
1377:. Archived from
1371:
1365:
1364:
1354:
1344:
1312:
1303:
1302:
1296:
1292:
1290:
1282:
1247:
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1212:
1206:
1197:
1191:
1190:
1180:
1170:
1138:
1132:
1131:
1115:
1105:
1090:Structural motif
1033:metalloproteases
1016:
994:triangular prism
975:
934:Dynamic features
879:β-sheets can be
678:structural motif
571:hydrogen bonding
526:
525:
515:
514:
477:
476:
466:
465:
424:
414:
403:hydrogen bonding
395:
385:
375:
364:hydrogen bonding
356:
264:
263:
252:
251:
78:
53:
43:
21:
2330:
2329:
2325:
2324:
2323:
2321:
2320:
2319:
2305:
2304:
2303:
2294:
2278:Supersecondary:
2273:
2230:
2205:
2176:
2173:
2135:Wayback Machine
2124:
2119:
2110:
2108:
2095:
2086:
2084:
2070:
2066:
2064:Further reading
2061:
2007:
2006:
2002:
1963:(7043): 773–8.
1950:
1949:
1945:
1901:
1900:
1896:
1889:
1876:
1875:
1871:
1834:(6793): 322–4.
1825:
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1547:Protein Science
1540:
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1490:Protein Science
1482:
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1423:
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1418:
1409:
1407:
1398:
1397:
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1327:(47): 17753–8.
1314:
1313:
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1271:
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1214:
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1128:
1107:
1106:
1102:
1098:
1061:
1041:
1030:
1008:
967:
960:
936:
885:flavodoxin fold
865:flavodoxin fold
861:hydrogen-bonded
853:
809:
796:
768:
766:β-meander motif
727:
715:protein folding
710:
708:Greek key motif
674:
672:β-hairpin motif
649:
601:
529:hydrogen-bonded
524:
519:
518:
517:
513:
508:
507:
506:
480:hydrogen-bonded
475:
470:
469:
468:
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459:
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457:
430:
429:
428:
427:
426:
420:
410:
396:
388:
387:
381:
371:
357:
346:
331:dihedral angles
307:dihedral angles
284:hydrogen-bonded
262:
256:
255:
254:
250:
245:
244:
243:
223:
218:
210:tautomerization
189:William Astbury
156:
148:proteinopathies
99:of the regular
93:β-pleated sheet
70:
48:
41:
28:
23:
22:
15:
12:
11:
5:
2328:
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2318:
2317:
2307:
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2261:
2256:
2255:
2254:
2244:
2238:
2236:
2232:
2231:
2229:
2228:
2226:Collagen helix
2223:
2218:
2213:
2208:
2203:
2199:
2193:
2191:
2184:
2178:
2177:
2174:
2172:
2171:
2164:
2157:
2149:
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2123:
2122:External links
2120:
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1914:(9): 3357–64.
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1065:Collagen helix
1060:
1057:
1045:amyloid plaque
1040:
1037:
959:
956:
940:hydrogen bonds
935:
932:
874:hydrogen bonds
852:
849:
808:
805:
795:
794:Psi-loop motif
792:
772:supersecondary
767:
764:
726:
723:
709:
706:
676:A very simple
673:
670:
648:
645:
600:
597:
520:
509:
484:peptide groups
471:
460:
442:hydrogen bonds
419:atoms colored
397:
390:
389:
380:atoms colored
358:
351:
350:
349:
348:
347:
345:
342:
293:Ramachandran (
257:
246:
235:hydrogen bonds
222:
219:
217:
214:
155:
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116:hydrogen bonds
95:) is a common
63:hydrogen bonds
26:
24:
14:
13:
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6:
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2:
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2027:
2023:
2020:(8): 3334–8.
2019:
2015:
2011:
2004:
2001:
1996:
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1604:
1601:(3): 203–12.
1600:
1596:
1589:
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1574:
1569:
1564:
1560:
1556:
1553:(2): 212–20.
1552:
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1427:
1420:
1417:
1406:on 2016-12-28
1405:
1401:
1395:
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1381:on 2012-02-04
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1234:
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1223:(3): 233–45.
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1174:
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1153:(5): 2754–9.
1152:
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1134:
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1127:0-471-19350-X
1123:
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1114:
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1081:
1078:
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1062:
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1046:
1038:
1036:
1034:
1028:
1024:
1023:pectate lyase
1015:
1011:
1005:
1001:
999:
995:
990:
988:
983:
974:
970:
964:
957:
955:
953:
949:
948:low-frequency
945:
941:
933:
931:
929:
925:
921:
917:
913:
909:
905:
901:
898:(such as the
897:
896:
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886:
882:
877:
875:
871:
866:
862:
858:
850:
848:
846:
842:
838:
834:
830:
829:All-β domains
826:
822:
818:
814:
806:
804:
802:
793:
791:
787:
785:
781:
777:
773:
765:
761:
756:
750:OspA β-sheet.
747:
743:
741:
737:
733:
724:
722:
720:
716:
707:
705:
703:
699:
695:
691:
687:
683:
679:
671:
665:
658:
653:
646:
644:
642:
638:
634:
630:
626:
622:
618:
614:
610:
609:phenylalanine
606:
598:
596:
594:
590:
586:
583:
578:
576:
572:
567:
563:
561:
556:
554:
550:
546:
542:
538:
534:
530:
523:
512:
503:
501:
497:
491:
489:
485:
481:
474:
463:
455:
451:
445:
443:
439:
435:
423:
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413:
408:
404:
400:
394:
384:
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343:
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308:
300:
296:
291:
287:
285:
281:
278:
277:
272:
268:
260:
249:
240:
236:
232:
228:
227:hydrogen bond
220:
215:
213:
211:
207:
203:
202:Linus Pauling
199:
194:
193:peptide bonds
190:
182:
178:
173:
169:
165:
160:
153:
151:
149:
145:
141:
137:
133:
129:
125:
121:
117:
114:
110:
106:
102:
98:
94:
90:
86:
77:
73:
68:
64:
60:
37:
32:
19:
2259:Beta hairpin
2241:
2109:. Retrieved
2105:the original
2100:
2085:. Retrieved
2081:the original
2076:
2017:
2013:
2003:
1960:
1956:
1946:
1911:
1907:
1897:
1878:
1872:
1831:
1827:
1821:
1778:
1774:
1764:
1739:
1735:
1729:
1694:
1690:
1680:
1648:(1): 236–9.
1645:
1641:
1631:
1598:
1594:
1550:
1546:
1536:
1493:
1489:
1478:
1433:
1429:
1419:
1408:. Retrieved
1404:the original
1394:
1383:. Retrieved
1379:the original
1369:
1324:
1320:
1252:
1245:
1220:
1216:
1210:
1195:
1150:
1146:
1136:
1112:Biochemistry
1111:
1103:
1053:
1042:
1039:In pathology
1020:
991:
979:
937:
911:
907:
892:
880:
878:
856:
854:
841:β-propellers
839:, β-prisms,
837:β-sandwiches
810:
797:
788:
784:β-propellers
769:
728:
711:
698:β-bulge loop
675:
636:
628:
602:
588:
579:
568:
564:
557:
552:
548:
544:
540:
536:
532:
521:
510:
504:
499:
495:
492:
487:
472:
461:
453:
449:
446:
431:
421:
411:
398:
382:
372:
360:Antiparallel
359:
339:
326:
322:
314:
310:
304:
298:
294:
274:
258:
247:
224:
206:Robert Corey
198:peptide bond
186:
180:
176:
164:antiparallel
138:observed in
128:conformation
108:
105:beta strands
104:
92:
88:
84:
82:
58:
2285:Coiled coil
1736:Biopolymers
1049:Alzheimer's
725:β-α-β motif
643:formation.
593:alpha helix
269:(0.60
140:amyloidosis
124:amino acids
120:polypeptide
18:Beta strand
2264:Beta bulge
1410:2007-05-31
1385:2007-06-01
1096:References
944:stretching
916:SH3 domain
900:TIM barrel
740:TIM barrel
625:isoleucine
613:tryptophan
560:amide ring
488:close pair
438:C-terminus
434:N-terminus
146:and other
85:beta sheet
2252:Beta turn
2235:Extended:
1510:1469-896X
1297:ignored (
1287:cite book
1070:Foldamers
904:β-Barrels
895:β-barrels
845:β-helices
833:β-barrels
831:may form
780:β-barrels
770:A simple
702:α-helices
682:β-hairpin
657:β-hairpin
617:threonine
549:wide pair
237:with the
109:β-strands
2309:Category
2269:α-strand
2242:β-strand
2190:Helices:
2131:Archived
1995:15944695
1856:10917536
1721:24304899
1623:28921557
1595:Proteins
1528:31306512
1470:20133689
1361:17093048
1187:11880627
1059:See also
1017:)
976:)
857:topology
825:peptides
803:family.
605:tyrosine
585:carbonyl
575:β-bulges
417:nitrogen
401:β-sheet
399:Parallel
378:nitrogen
362:β-sheet
280:peptides
221:Geometry
179:and the
168:catalase
113:backbone
2216:β-helix
2211:π-helix
2197:α-helix
2054:7682699
2022:Bibcode
1986:1479801
1965:Bibcode
1938:8253063
1864:4385352
1836:Bibcode
1813:4052563
1804:1329320
1783:Bibcode
1756:7115900
1712:3965108
1672:9016544
1615:2281084
1577:8745398
1568:2143354
1519:6699103
1461:2840449
1438:Bibcode
1352:1693819
1329:Bibcode
1279:7020376
1237:8506258
1202:. From
1155:Bibcode
1118:227–231
1085:α-helix
987:β-helix
982:β-helix
908:stagger
893:closed
887:or the
776:hairpin
719:meander
690:proline
686:glycine
641:amyloid
633:proline
582:peptide
498:,
452:,
325:,
313:,
297:,
154:History
132:fibrils
91:, also
89:β-sheet
2111:31 May
2087:25 May
2052:
2042:
1993:
1983:
1957:Nature
1936:
1929:413609
1926:
1885:
1862:
1854:
1828:Nature
1811:
1801:
1754:
1719:
1709:
1670:
1663:146380
1660:
1621:
1613:
1575:
1565:
1526:
1516:
1508:
1468:
1458:
1359:
1349:
1277:
1267:
1235:
1185:
1178:122420
1175:
1124:
843:, and
738:, the
629:middle
621:valine
407:Oxygen
368:Oxygen
309:near (
2206:helix
2045:46294
1860:S2CID
1619:S2CID
912:shear
813:all-β
732:β-α-β
696:or a
688:or a
659:motif
516:and C
467:and C
276:trans
253:and C
181:pleat
177:twist
97:motif
76:1AXC
2247:Turn
2113:2007
2089:2007
2050:PMID
1991:PMID
1934:PMID
1883:ISBN
1852:PMID
1809:PMID
1752:PMID
1717:PMID
1668:PMID
1611:PMID
1573:PMID
1524:PMID
1506:ISSN
1466:PMID
1357:PMID
1299:help
1275:PMID
1265:ISBN
1233:PMID
1183:PMID
1122:ISBN
1014:2PEC
998:LpxA
973:1QRE
881:open
855:The
819:and
782:and
694:turn
655:The
637:edge
589:same
569:The
436:and
422:blue
415:and
383:blue
376:and
335:BPTI
204:and
134:and
83:The
2040:PMC
2030:doi
1981:PMC
1973:doi
1961:435
1924:PMC
1916:doi
1844:doi
1832:406
1799:PMC
1791:doi
1744:doi
1707:PMC
1699:doi
1658:PMC
1650:doi
1603:doi
1563:PMC
1555:doi
1514:PMC
1498:doi
1456:PMC
1446:doi
1434:107
1347:PMC
1337:doi
1325:103
1257:doi
1225:doi
1173:PMC
1163:doi
1010:PDB
969:PDB
926:or
910:or
902:).
821:α/β
817:α+β
721:).
533:not
412:red
373:red
261:+ 2
239:C=O
231:N−H
172:PDB
142:,
72:PDB
65:in
61:of
2311::
2204:10
2099:.
2075:.
2048:.
2038:.
2028:.
2018:90
2016:.
2012:.
1989:.
1979:.
1971:.
1959:.
1955:.
1932:.
1922:.
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1910:.
1906:.
1858:.
1850:.
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1830:.
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1797:.
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1689:.
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1617:.
1609:.
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1585:^
1571:.
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619:,
611:,
607:,
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271:nm
212:.
150:.
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2168:e
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2056:.
2032::
2024::
1997:.
1975::
1967::
1940:.
1918::
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1815:.
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1165::
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553:j
545:j
541:j
537:i
522:j
511:i
500:ψ
496:φ
494:(
473:j
462:i
454:ψ
450:φ
425:.
386:.
327:ψ
323:φ
315:ψ
311:φ
299:ψ
295:φ
267:Å
259:i
248:i
170:(
107:(
87:(
20:)
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