17:
970:
41:
173:
Beta helices can associate with each other effectively, either face-to-face (mating the faces of their triangular prisms) or end-to-end (forming hydrogen bonds). Hence, β-helices can be used as "tags" to induce other proteins to associate, similar to
246:
Aik, WeiShen; McDonough, Michael A; Thalhammer, Armin; Chowdhury, Rasheduzzaman; Schofield, Christopher J (December 2012). "Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases".
748:
537:
119:
is 200 Å (20 nm) in length. Its interior is close-packed with no central pore and contains both hydrophobic residues and charged residues neutralized by
741:
356:
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".
599:
734:
530:
505:
500:
908:
1202:
523:
309:"A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila"
135:
763:
127:
85:
994:
222:
1043:
634:
158:
22:
1166:
715:
575:
77:
1207:
649:
546:
69:
1161:
959:
901:
1110:
365:
92:. Both left- and right-handed beta helices have been identified. These structures are distinct from
1171:
828:
629:
624:
182:
1142:
1090:
614:
389:
139:
1127:
16:
1105:
1095:
1053:
949:
802:
663:
639:
479:
430:
381:
338:
264:
52:
28:
1212:
1004:
894:
871:
594:
469:
461:
420:
409:"Crystal structure of beta-helical antifreeze protein points to a general ice binding model"
373:
328:
320:
256:
223:"CATH database - folds and homologous superfamilies within the beta 3-solenoid architecture"
203:"CATH database - folds and homologous superfamilies within the beta 2-solenoid architecture"
148:
46:
1137:
989:
939:
93:
369:
1068:
954:
807:
668:
589:
584:
565:
474:
449:
324:
153:
116:
425:
408:
333:
308:
40:
1196:
1147:
604:
227:
207:
112:
100:
81:
1122:
1117:
1063:
1009:
840:
699:
393:
96:, a different protein structure sometimes known as a "double-stranded beta helix".
76:
in a helical pattern with either two or three faces. The beta helix is a type of
1181:
1033:
984:
866:
850:
778:
683:
673:
658:
619:
560:
175:
120:
1155:
1058:
886:
845:
823:
726:
678:
260:
143:
73:
1176:
1100:
1025:
999:
944:
833:
783:
163:
108:
104:
483:
434:
385:
268:
342:
20:
Monomeric, left-handed β-helix antifreeze protein from the spruce budworm
1132:
1048:
792:
515:
130:
contain right-handed helices; left-handed versions have been observed in
510:
232:
202:
185:
family have been shown to possess a quadrilateral beta-helix structure.
282:
465:
56:
32:
917:
377:
131:
925:
921:
15:
44:
Dimeric, right-handed β-helix antifreeze protein from the beetle
307:
Kisker C, Schindelin H, Alber BE, Ferry JG, Rees DC (May 1996).
890:
730:
519:
448:
Vetting MW, Hegde SS, Fajardo JE, et al. (January 2006).
167:
89:
103:, which contains a seven-turn helix that reaches 34 Å (3.4
142:. Other proteins that contain beta helices include the
1083:
1018:
977:
932:
859:
816:
771:
762:
708:
692:
648:
574:
553:
99:The first beta-helix was observed in the enzyme
72:structure formed by the association of parallel
60:). Face-to-face association of β-helices.
80:. The structure is stabilized by inter-strand
902:
742:
531:
8:
111:tail spike protein, a component of the P22
1015:
909:
895:
887:
768:
749:
735:
727:
538:
524:
516:
473:
424:
407:Leinala EK, Davies PL, Jia Z (May 2002).
332:
166:on the β-helices bind to the surface of
115:, has 13 turns and in its assembled homo
39:
194:
136:UDP-N-acetylglucosamine acyltransferase
162:(left-handed), where regularly spaced
600:Transcription activator-like effector
501:SCOP family of right-handed β-helices
249:Current Opinion in Structural Biology
7:
506:SCOP family of left-handed β-helices
170:crystals and inhibit their growth.
325:10.1002/j.1460-2075.1996.tb00588.x
14:
968:
450:"Pentapeptide repeat proteins"
1:
426:10.1016/s0969-2126(02)00745-1
283:"Double-stranded beta-helix"
152:(right-handed) and from the
88:, and sometimes bound metal
86:protein-protein interactions
764:Protein secondary structure
757:Protein secondary structure
511:CATH β-helix protein family
1229:
966:
261:10.1016/j.sbi.2012.10.001
146:proteins from the beetle
635:Tetratricopeptide repeat
159:Choristoneura fumiferana
23:Choristoneura fumiferana
716:Repeated sequence (DNA)
126:Both pectate lyase and
78:solenoid protein domain
1203:Protein tandem repeats
547:Protein tandem repeats
61:
37:
128:P22 tailspike protein
70:tandem protein repeat
43:
19:
630:Pentapeptide repeat
625:Leucine-rich repeat
370:2000Natur.406..322L
183:pentapeptide repeat
693:Beads-on-a-string:
615:Antifreeze protein
140:carbonic anhydrase
62:
38:
1190:
1189:
1079:
1078:
884:
883:
880:
879:
803:Polyproline helix
724:
723:
664:Beta trefoil fold
640:Trefoil knot fold
466:10.1021/bi052130w
1220:
1016:
995:Boerdijk–Coxeter
972:
971:
911:
904:
897:
888:
872:Helix-turn-helix
769:
751:
744:
737:
728:
595:Armadillo repeat
540:
533:
526:
517:
488:
487:
477:
445:
439:
438:
428:
404:
398:
397:
378:10.1038/35018604
353:
347:
346:
336:
304:
298:
297:
295:
293:
279:
273:
272:
243:
237:
236:
235:on 26 July 2011.
231:. Archived from
219:
213:
212:
199:
149:Tenebrio molitor
94:jelly-roll folds
59:
47:Tenebrio molitor
35:
1228:
1227:
1223:
1222:
1221:
1219:
1218:
1217:
1193:
1192:
1191:
1186:
1075:
1029:
1014:
973:
969:
964:
928:
915:
885:
876:
860:Supersecondary:
855:
812:
787:
758:
755:
725:
720:
704:
688:
644:
570:
549:
544:
497:
492:
491:
447:
446:
442:
406:
405:
401:
364:(6793): 322–4.
355:
354:
350:
319:(10): 2323–30.
306:
305:
301:
291:
289:
281:
280:
276:
245:
244:
240:
221:
220:
216:
201:
200:
196:
191:
181:Members of the
51:
27:
12:
11:
5:
1226:
1224:
1216:
1215:
1210:
1205:
1195:
1194:
1188:
1187:
1185:
1184:
1179:
1174:
1169:
1164:
1159:
1152:
1151:
1150:
1140:
1135:
1130:
1125:
1120:
1115:
1114:
1113:
1108:
1103:
1093:
1087:
1085:
1081:
1080:
1077:
1076:
1074:
1073:
1072:
1071:
1061:
1056:
1051:
1046:
1041:
1036:
1031:
1027:
1022:
1020:
1013:
1012:
1007:
1002:
997:
992:
987:
981:
979:
975:
974:
967:
965:
963:
962:
957:
952:
947:
942:
936:
934:
930:
929:
916:
914:
913:
906:
899:
891:
882:
881:
878:
877:
875:
874:
869:
863:
861:
857:
856:
854:
853:
848:
843:
838:
837:
836:
826:
820:
818:
814:
813:
811:
810:
808:Collagen helix
805:
800:
795:
790:
785:
781:
775:
773:
766:
760:
759:
756:
754:
753:
746:
739:
731:
722:
721:
719:
718:
712:
710:
706:
705:
703:
702:
696:
694:
690:
689:
687:
686:
681:
676:
671:
669:Beta-propeller
666:
661:
655:
653:
646:
645:
643:
642:
637:
632:
627:
622:
617:
612:
607:
602:
597:
592:
590:Ankyrin repeat
587:
585:Alpha solenoid
581:
579:
572:
571:
569:
568:
566:Collagen helix
563:
557:
555:
551:
550:
545:
543:
542:
535:
528:
520:
514:
513:
508:
503:
496:
495:External links
493:
490:
489:
440:
399:
348:
299:
274:
255:(6): 691–700.
238:
214:
193:
192:
190:
187:
154:spruce budworm
82:hydrogen bonds
13:
10:
9:
6:
4:
3:
2:
1225:
1214:
1211:
1209:
1208:Protein folds
1206:
1204:
1201:
1200:
1198:
1183:
1180:
1178:
1175:
1173:
1170:
1168:
1165:
1163:
1160:
1158:
1157:
1153:
1149:
1146:
1145:
1144:
1141:
1139:
1136:
1134:
1131:
1129:
1126:
1124:
1121:
1119:
1116:
1112:
1109:
1107:
1104:
1102:
1099:
1098:
1097:
1094:
1092:
1089:
1088:
1086:
1082:
1070:
1067:
1066:
1065:
1062:
1060:
1057:
1055:
1052:
1050:
1047:
1045:
1042:
1040:
1037:
1035:
1032:
1030:
1024:
1023:
1021:
1017:
1011:
1008:
1006:
1003:
1001:
998:
996:
993:
991:
988:
986:
983:
982:
980:
976:
961:
958:
956:
953:
951:
948:
946:
943:
941:
938:
937:
935:
931:
927:
923:
919:
912:
907:
905:
900:
898:
893:
892:
889:
873:
870:
868:
865:
864:
862:
858:
852:
849:
847:
844:
842:
839:
835:
832:
831:
830:
827:
825:
822:
821:
819:
815:
809:
806:
804:
801:
799:
796:
794:
791:
789:
782:
780:
777:
776:
774:
770:
767:
765:
761:
752:
747:
745:
740:
738:
733:
732:
729:
717:
714:
713:
711:
707:
701:
698:
697:
695:
691:
685:
682:
680:
677:
675:
672:
670:
667:
665:
662:
660:
657:
656:
654:
651:
647:
641:
638:
636:
633:
631:
628:
626:
623:
621:
618:
616:
613:
611:
608:
606:
605:Beta solenoid
603:
601:
598:
596:
593:
591:
588:
586:
583:
582:
580:
577:
573:
567:
564:
562:
559:
558:
556:
552:
548:
541:
536:
534:
529:
527:
522:
521:
518:
512:
509:
507:
504:
502:
499:
498:
494:
485:
481:
476:
471:
467:
463:
459:
455:
451:
444:
441:
436:
432:
427:
422:
419:(5): 619–27.
418:
414:
410:
403:
400:
395:
391:
387:
383:
379:
375:
371:
367:
363:
359:
352:
349:
344:
340:
335:
330:
326:
322:
318:
314:
310:
303:
300:
288:
284:
278:
275:
270:
266:
262:
258:
254:
250:
242:
239:
234:
230:
229:
228:CATH database
224:
218:
215:
210:
209:
208:CATH database
204:
198:
195:
188:
186:
184:
179:
177:
171:
169:
165:
161:
160:
155:
151:
150:
145:
141:
138:and archaeal
137:
133:
129:
124:
122:
118:
114:
113:bacteriophage
110:
106:
102:
101:pectate lyase
97:
95:
91:
87:
83:
79:
75:
71:
67:
58:
54:
49:
48:
42:
34:
30:
25:
24:
18:
1154:
1038:
1019:Biochemistry
841:Beta hairpin
797:
700:Sushi domain
609:
457:
454:Biochemistry
453:
443:
416:
412:
402:
361:
357:
351:
316:
312:
302:
290:. Retrieved
286:
277:
252:
248:
241:
233:the original
226:
217:
206:
197:
180:
172:
157:
147:
125:
121:salt bridges
107:) long. The
98:
65:
63:
45:
21:
1167:Pitch angle
1143:Logarithmic
1091:Archimedean
1054:Polyproline
867:Coiled coil
684:WD40 repeat
674:Kelch motif
659:Beta barrel
620:HEAT repeat
561:Coiled coil
460:(1): 1–10.
292:29 November
176:coiled coil
1197:Categories
1156:On Spirals
1106:Hyperbolic
846:Beta bulge
679:TIM barrel
610:Beta helix
189:References
178:segments.
164:threonines
144:antifreeze
74:beta sheet
66:beta helix
1177:Spirangle
1172:Theodorus
1111:Poinsot's
1101:Epispiral
945:Curvature
940:Algebraic
834:Beta turn
817:Extended:
709:See also:
576:Elongated
413:Structure
109:P22 phage
36:).
1133:Involute
1128:Fermat's
1069:Collagen
1005:Symmetry
851:α-strand
824:β-strand
772:Helices:
554:Fibrous:
484:16388575
435:12015145
386:10917536
269:23142576
134:such as
1213:Helices
1162:Padovan
1096:Cotes's
1084:Spirals
990:Antenna
978:Helices
950:Gallery
926:helices
918:Spirals
798:β-helix
793:π-helix
779:α-helix
475:2566302
394:4385352
366:Bibcode
343:8665839
132:enzymes
1148:Golden
1064:Triple
1044:Double
1010:Triple
960:Topics
933:Curves
922:curves
650:Closed
482:
472:
433:
392:
384:
358:Nature
341:
334:450161
331:
313:EMBO J
267:
117:trimer
1123:Euler
1118:Doyle
1059:Super
1034:Alpha
985:Angle
788:helix
390:S2CID
287:SCOPe
68:is a
1182:Ulam
1138:List
1039:Beta
1000:Hemi
955:List
924:and
829:Turn
480:PMID
431:PMID
382:PMID
339:PMID
294:2021
265:PMID
90:ions
57:1EZG
33:1M8N
470:PMC
462:doi
421:doi
374:doi
362:406
329:PMC
321:doi
257:doi
168:ice
53:PDB
29:PDB
1199::
1049:Pi
1028:10
920:,
786:10
478:.
468:.
458:45
456:.
452:.
429:.
417:10
415:.
411:.
388:.
380:.
372:.
360:.
337:.
327:.
317:15
315:.
311:.
285:.
263:.
253:22
251:.
225:.
205:.
156:,
123:.
105:nm
84:,
64:A
55::
31::
1026:3
910:e
903:t
896:v
784:3
750:e
743:t
736:v
652::
578::
539:e
532:t
525:v
486:.
464::
437:.
423::
396:.
376::
368::
345:.
323::
296:.
271:.
259::
211:.
50:(
26:(
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
