942:
a set of theoretical parameters for each conformation based on the structure. Conformational subsets from this pool whose average theoretical parameters closely match known experimental data for this protein are selected. The alternative molecular dynamics approach takes multiple random conformations at a time and subjects all of them to experimental data. Here the experimental data is serving as limitations to be placed on the conformations (e.g. known distances between atoms). Only conformations that manage to remain within the limits set by the experimental data are accepted. This approach often applies large amounts of experimental data to the conformations which is a very computationally demanding task.
124:
893:
1080:
1069:
135:
981:
322:
27:
656:
3185:
445:
643:. Hundreds of proteins have been identified as being assembled into homomers in human cells. The process of assembly is often initiated by the interaction of the N-terminal region of polypeptide chains. Evidence that numerous gene products form homomers (multimers) in a variety of organisms based on
941:
that fall into two general methodologies – pool and molecular dynamics (MD) approaches (diagrammed in the figure). The pool based approach uses the protein's amino acid sequence to create a massive pool of random conformations. This pool is then subjected to more computational processing that creates
1176:
protein structures. The aim of most protein structure databases is to organize and annotate the protein structures, providing the biological community access to the experimental data in a useful way. Data included in protein structure databases often includes 3D coordinates as well as experimental
1181:
determined structures. Though most instances, in this case either proteins or a specific structure determinations of a protein, also contain sequence information and some databases even provide means for performing sequence based queries, the primary attribute of a structure database is structural
932:
files are a representation of a protein that can be considered to have a flexible structure. Creating these files requires determining which of the various theoretically possible protein conformations actually exist. One approach is to apply computational algorithms to the protein data in order to
1257:
is much easier than the determination of a protein structure. However, the structure of a protein gives much more insight in the function of the protein than its sequence. Therefore, a number of methods for the computational prediction of protein structure from its sequence have been developed.
1059:
may result in loss of function, and loss of native state. The free energy of stabilization of soluble globular proteins typically does not exceed 50 kJ/mol. Taking into consideration the large number of hydrogen bonds that take place for the stabilization of secondary structures, and the
607:, such as a 2-fold axis in a dimer. Multimers made up of identical subunits are referred to with a prefix of "homo-" and those made up of different subunits are referred to with a prefix of "hetero-", for example, a heterotetramer, such as the two alpha and two beta chains of
1119:
can determine protein structures. The resolution is typically lower than that of X-ray crystallography, or NMR, but the maximum resolution is steadily increasing. This technique is still a particularly valuable for very large protein complexes such as
485:. Both the α-helix and the β-sheet represent a way of saturating all the hydrogen bond donors and acceptors in the peptide backbone. Some parts of the protein are ordered but do not form any regular structures. They should not be confused with
1218:
database provide two different structural classifications of proteins. When the structural similarity is large the two proteins have possibly diverged from a common ancestor, and shared structure between proteins is considered evidence of
404:, establishing that proteins have defining amino acid sequences. The sequence of a protein is unique to that protein, and defines the structure and function of the protein. The sequence of a protein can be determined by methods such as
904:
that experience conformational changes after being affected by interactions with other proteins or as a part of enzymatic activity. However, proteins may have varying degrees of stability, and some of the less stable variants are
1152:, can probe the structured fraction and its stability without the need for purification. Once a protein's structure has been experimentally determined, further detailed studies can be done computationally, using
1143:
has become a valuable method to investigate the structures of flexible peptides and proteins that cannot be studied with other methods. A more qualitative picture of protein structure is often obtained by
2379:
703:
but instead appear in a variety of proteins. Domains often are named and singled out because they figure prominently in the biological function of the protein they belong to; for example, the "
1551:
Chiang YS, Gelfand TI, Kister AE, Gelfand IM (September 2007). "New classification of supersecondary structures of sandwich-like proteins uncovers strict patterns of strand assemblage".
575:
Quaternary structure is the three-dimensional structure consisting of the aggregation of two or more individual polypeptide chains (subunits) that operate as a single functional unit (
583:
and disulfide bonds as in tertiary structure. There are many possible quaternary structure organisations. Complexes of two or more polypeptides (i.e. multiple subunits) are called
1194:, both in developing the computational methods used and in providing a large experimental dataset used by some methods to provide insights about the function of a protein.
2516:
Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H, Phillips DC (March 1958). "A three-dimensional model of the myoglobin molecule obtained by x-ray analysis".
1231:, and joining proteins sharing these fragments into protein superfamilies is no longer justified. Topology of a protein can be used to classify proteins as well.
635:. Bertolini et al. in 2021 presented evidence that homomer formation may be driven by interaction between nascent polypeptide chains as they are translated from
130:
1227:. If shared structure is significant but the fraction shared is small, the fragment shared may be the consequence of a more dramatic evolutionary event such as
1186:
focus on sequence information, and contain no structural information for the majority of entries. Protein structure databases are critical for many efforts in
873:. "n effect, the is a nanomachine composed of perhaps over 600 proteins in molecular complexes, many of which also function independently as nanomachines...
225:, rather than a protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of
128:
3741:
2305:
Sivakolundu SG, Bashford D, Kriwacki RW (November 2005). "Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation".
129:
3913:
3882:
3826:
3774:
1060:
stabilization of the inner core through hydrophobic interactions, the free energy of stabilization emerges as small difference between large numbers.
127:
1055:
protein states. This free energy difference is very sensitive to temperature, hence a change in temperature may result in unfolding or denaturation.
4025:
1449:
Sanger F (May 1959). "Chemistry of insulin; determination of the structure of insulin opens the way to greater understanding of life processes".
2810:
Kumari I, Sandhu P, Ahmed M, Akhter Y (August 2017). "Molecular
Dynamics Simulations, Challenges and Opportunities: A Biologist's Prospective".
481:
between the main-chain peptide groups. They have a regular geometry, being constrained to specific values of the dihedral angles ψ and φ on the
3002:"Cross-over between discrete and continuous protein structure space: insights into automatic classification and networks of protein structures"
1211:
784:
743:
refer to short segments of protein three-dimensional structure or amino acid sequence that were found in a large number of different proteins
2093:"Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase"
1270:
methods can build a 3-D model for a protein of unknown structure from experimental structures of evolutionarily-related proteins, called a
372:-group), which is the end where the amino group is not involved in a peptide bond. The primary structure of a protein is determined by the
2340:
Zhang G, Ignatova Z (February 2011). "Folding at the birth of the nascent chain: coordinating translation with co-translational folding".
1796:
1239:
are two topology frameworks developed for classification of protein folds based on chain crossing and intrachain contacts respectively.
3163:
2258:"A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein"
1178:
664:
2901:
416:. It is strictly recommended to use the words "amino acid residues" when discussing proteins because when a peptide bond is formed, a
3734:
3404:
141:
1780:
3217:
546:
489:, an unfolded polypeptide chain lacking any fixed three-dimensional structure. Several sequential secondary structures may form a "
461:
refers to highly regular local sub-structures on the actual polypeptide backbone chain. Two main types of secondary structure, the
368:(N-terminus) based on the nature of the free group on each extremity. Counting of residues always starts at the N-terminal end (NH
2142:"p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins"
1402:"The amino-acid sequence in the phenylalanyl chain of insulin. I. The identification of lower peptides from partial hydrolysates"
91:
3601:
63:
2391:
1335:
1140:
1148:, which is also useful to screen for more crystallizable protein samples. Novel implementations of this approach, including
4123:
4018:
3727:
3651:
3189:
2644:"Identifying residual structure in intrinsically disordered systems: a 2D IR spectroscopic study of the GVGXPGVG peptide"
296:
272:
Protein structures range in size from tens to several thousand amino acids. By physical size, proteins are classified as
70:
886:
1149:
44:
4128:
4118:
3810:
3596:
2598:
1951:
1861:
1632:
Bertolini M, Fenzl K, Kats I, Wruck F, Tippmann F, Schmitt J, Auburger JJ, Tans S, Bukau B, Kramer G (January 2021).
922:
906:
110:
3161:
50 Years of
Protein Structure Determination Timeline - HTML Version - National Institute of General Medical Sciences
945:
The conformational ensembles were generated for a number of highly dynamic and partially unfolded proteins, such as
4108:
3836:
302:
in performing its biological function. The alternative structures of the same protein are referred to as different
266:
77:
921:
have been devised as a way to provide a more accurate and 'dynamic' representation of the conformational state of
4113:
4011:
3929:
3784:
3611:
3245:
2581:
Krimm S, Bandekar J (1986). "Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins".
950:
421:
245:
packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their
3519:
878:
48:
892:
59:
3872:
3764:
3474:
3397:
1029:. The final structure of the protein chain is generally assumed to be determined by its amino acid sequence (
262:
3867:
432:
are usually also considered a part of the primary structure, and cannot be read from the gene. For example,
409:
4075:
4065:
3993:
3971:
3210:
2140:
De Biasio A, Ibáñez de Opakua A, Cordeiro TN, Villate M, Merino N, Sibille N, et al. (February 2014).
1263:
1248:
1111:
to be determined to a certain resolution. Roughly 7% of the known protein structures have been obtained by
720:
695:
independently of the rest of the protein chain. Many domains are not unique to the protein products of one
570:
436:
is composed of 51 amino acids in 2 chains. One chain has 31 amino acids, and the other has 20 amino acids.
2902:"SCOP: a structural classification of proteins database for the investigation of sequences and structures"
671:
Proteins are frequently described as consisting of several structural units. These units include domains,
4138:
4055:
1841:
1056:
1052:
453:
2696:"Two-dimensional infrared population transfer spectroscopy for enhancing structural markers of proteins"
1848:. Advances in Protein Chemistry and Structural Biology. Vol. 83. Academic Press. pp. 163–221.
992:
4223:
4060:
3988:
3663:
1165:
914:
910:
901:
660:
644:
502:
246:
2671:
4194:
4050:
3934:
335:
2628:
751:
Tertiary protein structures can have multiple secondary elements on the same polypeptide chain. The
3877:
3779:
3390:
1228:
1136:
1116:
934:
929:
918:
752:
580:
526:
490:
385:
303:
226:
719:
proteins. A conservative combination of several domains that occur in different proteins, such as
603:
if it contains five subunits, and so forth. The subunits are frequently related to one another by
3898:
3851:
3203:
2643:
2079:
938:
37:
1594:
Moutevelis E, Woolfson DN (January 2009). "A periodic table of coiled-coil protein structures".
1494:"The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain"
4095:
4085:
4034:
2197:
Kragelj J, Palencia A, Nanao MH, Maurin D, Bouvignies G, Blackledge M, Jensen MR (March 2015).
1826:
1634:"Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly"
1293:
1283:
1079:
672:
84:
1325:
4103:
3955:
3939:
3908:
3769:
3554:
3349:
2407:
1224:
1187:
1092:
1042:
826:
814:
806:
397:
307:
299:
254:
206:
3240:
3160:
3013:
2932:
2764:
2707:
2525:
2472:
2210:
2153:
2031:"Computational approaches for inferring the functions of intrinsically disordered proteins"
1898:
1505:
1458:
1139:
can also be used to characterize the conformation of peptides, polypeptides, and proteins.
675:, and folds. Despite the fact that there are about 100,000 different proteins expressed in
530:
353:
238:
2753:"Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp"
865:, which moves cargo inside cells towards the nucleus and produces the axonemal beating of
8:
4207:
4164:
4133:
3976:
3636:
1191:
1030:
756:
712:
510:
refers to the three-dimensional structure created by a single protein molecule (a single
458:
205:, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing
3017:
2768:
2711:
2529:
2476:
2465:
Philosophical
Transactions of the Royal Society of London. Series B, Biological Sciences
2214:
2157:
1902:
1509:
1462:
1095:. This method allows one to measure the three-dimensional (3-D) density distribution of
909:. These proteins exist and function in a relatively 'disordered' state lacking a stable
3903:
3831:
3703:
3621:
3134:
3109:
3085:
3060:
3036:
3001:
2870:
2787:
2752:
2728:
2695:
2616:
2549:
2490:
2436:
2411:
2282:
2257:
2233:
2198:
2174:
2141:
2117:
2092:
2057:
2030:
2001:
1976:
1919:
1886:
1853:
1818:
1756:
1731:
1707:
1682:
1658:
1633:
1576:
1528:
1493:
1426:
1401:
1377:
1352:
1220:
1153:
1132:
1121:
830:
592:
519:
507:
250:
170:
2974:
2957:
2920:
2823:
2590:
2091:
Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, et al. (March 2010).
659:
Protein domains. The two shown protein structures share a common domain (maroon), the
3805:
3800:
3698:
3255:
3139:
3090:
3041:
2979:
2924:
2889:
2862:
2827:
2792:
2733:
2676:
2604:
2594:
2541:
2498:
2441:
2387:
2357:
2322:
2287:
2238:
2179:
2122:
2062:
2006:
1957:
1947:
1924:
1867:
1857:
1810:
1761:
1712:
1683:"INTRAGENIC COMPLEMENTATION AMONG TEMPERATURE SENSITIVE MUTANTS OF BACTERIOPHAGE T4D"
1663:
1611:
1568:
1533:
1474:
1431:
1382:
1331:
1267:
1183:
1088:
1073:
1048:
716:
688:
588:
511:
482:
405:
361:
357:
341:
277:
234:
214:
154:
2874:
1580:
691:
is an element of the protein's overall structure that is self-stabilizing and often
4189:
3688:
3359:
3317:
3312:
3307:
3129:
3121:
3080:
3072:
3031:
3021:
2969:
2949:
2916:
2854:
2819:
2782:
2772:
2723:
2715:
2666:
2658:
2586:
2553:
2533:
2480:
2431:
2423:
2349:
2314:
2277:
2269:
2256:
Allison JR, Rivers RC, Christodoulou JC, Vendruscolo M, Dobson CM (November 2014).
2228:
2218:
2169:
2161:
2112:
2104:
2052:
2042:
1996:
1988:
1914:
1906:
1849:
1822:
1800:
1792:
1751:
1743:
1702:
1694:
1653:
1645:
1603:
1560:
1523:
1513:
1466:
1421:
1413:
1372:
1364:
1254:
1236:
1203:
822:
818:
810:
800:
788:
760:
736:
401:
230:
2642:
Lessing J, Roy S, Reppert M, Baer M, Marx D, Jansen TL, et al. (March 2012).
1470:
3265:
3250:
3167:
3026:
2777:
1012:
874:
834:
692:
425:
281:
2719:
1698:
4159:
4080:
3626:
3489:
3413:
3286:
2953:
2203:
Proceedings of the
National Academy of Sciences of the United States of America
1498:
Proceedings of the
National Academy of Sciences of the United States of America
1303:
1288:
1271:
962:
838:
740:
604:
550:
538:
515:
478:
417:
365:
210:
3719:
3125:
2858:
2353:
2318:
2165:
2108:
1992:
1607:
679:
systems, there are many fewer different domains, structural motifs and folds.
412:. Often, however, it is read directly from the sequence of the gene using the
4217:
3559:
3344:
3339:
2897:
2375:
2047:
1961:
1885:
Fraser JS, Clarkson MW, Degnan SC, Erion R, Kern D, Alber T (December 2009).
1169:
1068:
780:
636:
474:
429:
349:
289:
2223:
1887:"Hidden alternative structures of proline isomerase essential for catalysis"
1842:"Proteins MOVE! Protein dynamics and long-range allostery in cell signaling"
1649:
4174:
3846:
3641:
3564:
3549:
3509:
3444:
3143:
3094:
3045:
2866:
2831:
2796:
2737:
2680:
2545:
2485:
2460:
2361:
2326:
2291:
2242:
2183:
2126:
2066:
2010:
1928:
1871:
1814:
1797:
10.1002/(SICI)1097-0134(19990601)35:4<408::AID-PROT4>3.0.CO;2-A
1765:
1716:
1667:
1615:
1572:
1537:
1478:
1435:
1386:
1100:
1026:
858:
854:
772:
413:
273:
218:
2983:
2928:
2608:
2502:
2445:
1518:
881:
connected by them to recruit their binding partners and induce long-range
866:
553:. The disulfide bonds are extremely rare in cytosolic proteins, since the
4003:
3708:
3693:
3616:
3606:
3586:
3581:
3576:
3539:
3494:
3469:
3454:
3449:
3434:
3364:
3354:
3076:
2893:
1805:
1368:
1232:
1145:
1112:
1022:
776:
700:
620:
486:
466:
462:
258:
242:
190:
2139:
1910:
1223:. Structure similarity can then be used to group proteins together into
1202:
Protein structures can be grouped based on their structural similarity,
980:
4169:
3841:
3683:
3678:
3673:
3658:
3646:
3631:
3571:
3544:
3534:
3529:
3524:
3514:
3484:
3479:
3464:
3459:
3439:
3429:
3291:
2494:
1564:
708:
676:
608:
470:
377:
345:
221:. By convention, a chain under 30 amino acids is often identified as a
194:
174:
2662:
2427:
2273:
1417:
711:". Because they are independently stable, domains can be "swapped" by
158:
16:
Three-dimensional arrangement of atoms in an amino acid-chain molecule
3668:
3591:
3504:
3499:
3424:
3369:
2567:
2537:
2255:
1747:
1732:"Superdomains in the protein structure hierarchy: The case of PTP-C2"
1207:
882:
724:
624:
420:
is lost, and therefore proteins are made up of amino acid residues.
348:
in the polypeptide chain. The primary structure is held together by
321:
26:
3322:
3260:
1298:
1096:
1018:
954:
870:
727:
pair, was called "a superdomain" that may evolve as a single unit.
640:
632:
628:
600:
596:
584:
576:
393:
178:
3382:
813:, and have been linked to functionally relevant phenomena such as
805:
Proteins are not static objects, but rather populate ensembles of
771:
A protein fold refers to the general protein architecture, like a
763:
motif. Some of them may be also referred to as structural motifs.
655:
650:
201:
of the polymer. A single amino acid monomer may also be called a
4154:
3332:
3327:
3226:
1125:
850:
704:
554:
433:
222:
198:
186:
182:
2958:"CATH--a hierarchic classification of protein domain structures"
1242:
913:. As a result, they are difficult to describe by a single fixed
794:
134:
3184:
2999:
1778:
966:
958:
862:
846:
842:
518:. The α-helices and β-pleated-sheets are folded into a compact
1131:
General secondary structure composition can be determined via
444:
3000:
Pascual-García A, Abia D, Ortiz AR, Bastolla U (March 2009).
1104:
933:
try to determine the most likely set of conformations for an
558:
534:
285:
937:
file. There are multiple methods for preparing data for the
896:
Schematic view of the two main ensemble modeling approaches.
3195:
2887:
2378:, Johnson A, Lewis J, Raff M, Roberts K, Walters P (2002).
2304:
1215:
1108:
946:
696:
549:, hydrogen bonds, and the tight packing of side chains and
400:. The sequence of amino acids in insulin was discovered by
389:
373:
149:
2199:"Structure and dynamics of the MKK7-JNK signaling complex"
2196:
2090:
2029:
Varadi M, Vranken W, Guharoy M, Tompa P (1 January 2015).
1550:
1083:
Rate of
Protein Structure Determination by Method and Year
4184:
4179:
3171:
3110:"Progress and challenges in protein structure prediction"
2845:
Laskowski RA (June 2011). "Protein structure databases".
2515:
2386:(Fourth ed.). New York and London: Garland Science.
2028:
1884:
1262:
prediction methods use just the sequence of the protein.
1197:
1177:
information, such as unit cell dimensions and angles for
381:
1779:
Govindarajan S, Recabarren R, Goldstein RA (June 1999).
1353:"Protein length in eukaryotic and prokaryotic proteomes"
477:. These secondary structures are defined by patterns of
2809:
2374:
1631:
537:, but the structure is stable only when the parts of a
2948:
2412:"The formation and stabilization of protein structure"
1680:
1087:
Around 90% of the protein structures available in the
809:. Transitions between these states typically occur on
2641:
376:
corresponding to the protein. A specific sequence of
318:
There are four distinct levels of protein structure.
4070:
2461:"Protein structure and function at low temperatures"
1946:(4th ed.). Hoboken, NJ: John Wiley & Sons.
1173:
579:). The resulting multimer is stabilized by the same
2750:
1491:
1047:Thermodynamic stability of proteins represents the
900:Proteins are often thought of as relatively stable
51:. Unsourced material may be challenged and removed.
1593:
1063:
730:
619:An assemblage of multiple copies of a particular
4215:
1974:
1681:BERNSTEIN H, EDGAR RS, DENHARDT GH (June 1965).
1350:
1115:(NMR) techniques. For larger protein complexes,
3749:
1627:
1625:
853:, which moves cargo inside cells away from the
651:Domains, motifs, and folds in protein structure
249:. This is the topic of the scientific field of
126:
3058:
2995:
2993:
2952:, Michie AD, Jones S, Jones DT, Swindells MB,
2693:
1781:"Estimating the total number of protein folds"
1492:Pauling L, Corey RB, Branson HR (April 1951).
1212:Structural Classification of Proteins database
1159:
785:Structural Classification of Proteins database
313:
4019:
3735:
3398:
3211:
2580:
2339:
1772:
1344:
1243:Computational prediction of protein structure
795:Protein dynamics and conformational ensembles
2803:
2744:
1833:
1622:
448:An α-helix with hydrogen bonds (yellow dots)
193: – formed from sequences of
2990:
2942:
2881:
2574:
1977:"Structure and function of mammalian cilia"
1587:
1544:
1399:
1017:As it is translated, polypeptides exit the
746:
4033:
4026:
4012:
3742:
3728:
3405:
3391:
3218:
3204:
2672:11370/ff19c09b-088a-48f0-afee-2111a9b19252
1839:
1485:
665:phosphatidylinositol (3,4,5)-trisphosphate
306:, and transitions between them are called
269:, to determine the structure of proteins.
3133:
3101:
3084:
3061:"Dali server: conservation mapping in 3D"
3035:
3025:
2973:
2844:
2786:
2776:
2751:Minde DP, Maurice MM, Rüdiger SG (2012).
2727:
2670:
2484:
2435:
2281:
2232:
2222:
2173:
2116:
2056:
2046:
2000:
1968:
1918:
1804:
1755:
1729:
1706:
1657:
1527:
1517:
1425:
1376:
1317:
217:in order to attach to one another with a
111:Learn how and when to remove this message
2651:Journal of the American Chemical Society
2458:
2406:
2400:
1941:
1078:
1072:Examples of protein structures from the
1067:
891:
829:allow proteins to function as nanoscale
715:between one protein and another to make
654:
443:
320:
138:The image above contains clickable links
122:
2583:Advances in Protein Chemistry Volume 38
2368:
1351:Brocchieri L, Karlin S (10 June 2005).
1306:3D schematic representation of proteins
564:
344:of a protein refers to the sequence of
4216:
1448:
1323:
1198:Structural classifications of proteins
439:
171:three-dimensional arrangement of atoms
4007:
3723:
3386:
3199:
3114:Current Opinion in Structural Biology
3107:
2812:Current Protein & Peptide Science
2380:"The Shape and Structure of Proteins"
2342:Current Opinion in Structural Biology
2024:
2022:
2020:
1975:Satir P, Christensen ST (June 2008).
1141:Two-dimensional infrared spectroscopy
783:or different "folds" provided in the
557:(intracellular fluid) is generally a
496:
2694:Jansen TL, Knoester J (March 2008).
1400:Sanger F, Tuppy H (September 1951).
1036:
975:
755:refers to a specific combination of
682:
599:if it contains four subunits, and a
587:. Specifically it would be called a
352:that are made during the process of
329:
276:, between 1–100 nm. Very large
209:, in which the amino acids lose one
49:adding citations to reliable sources
20:
3412:
833:within cells, often in the form of
759:elements, such as β-α-β units or a
253:, which employs techniques such as
13:
3154:
3059:Holm L, Rosenström P (July 2010).
2585:. Vol. 38. pp. 181–364.
2035:Frontiers in Molecular Biosciences
2017:
1854:10.1016/B978-0-12-381262-9.00005-7
1150:fast parallel proteolysis (FASTpp)
971:
263:cryo-electron microscopy (cryo-EM)
133:
14:
4235:
3177:
2824:10.2174/1389203718666170622074741
1330:. Cengage Learning. p. 371.
923:intrinsically disordered proteins
907:intrinsically disordered proteins
595:if it contains three subunits, a
284:. For example, many thousands of
3837:Dual-polarization interferometry
3183:
1327:Organic and Biological Chemistry
979:
422:Post-translational modifications
325:Four levels of protein structure
267:dual polarisation interferometry
189: – specifically
25:
3246:Post-translational modification
3071:(Web Server issue): W545–W549.
3052:
2838:
2687:
2635:
2560:
2509:
2452:
2333:
2298:
2249:
2190:
2133:
2084:
2073:
1981:Histochemistry and Cell Biology
1935:
1878:
1723:
1156:simulations of that structure.
1107:the 3-D coordinates of all the
1064:Protein structure determination
766:
647:evidence was reviewed in 1965.
591:if it contains two subunits, a
545:tertiary interactions, such as
522:. The folding is driven by the
36:needs additional citations for
3868:Analytical ultracentrifugation
1846:Protein Structure and Diseases
1674:
1442:
1393:
731:Structural and sequence motifs
1:
3873:Size exclusion chromatography
3765:Cryogenic electron microscopy
2975:10.1016/S0969-2126(97)00260-8
2921:10.1016/S0022-2836(05)80134-2
2591:10.1016/S0065-3233(08)60528-8
2384:Molecular Biology of the Cell
1730:Haynie DT, Xue B (May 2015).
1471:10.1126/science.129.3359.1340
1310:
3972:Protein structure prediction
3225:
3027:10.1371/journal.pcbi.1000331
2909:Journal of Molecular Biology
2778:10.1371/journal.pone.0046147
2307:Journal of Molecular Biology
1596:Journal of Molecular Biology
1324:Stoker HS (1 January 2015).
1249:Protein structure prediction
721:protein tyrosine phosphatase
623:chain can be described as a
571:Protein quaternary structure
473:, were suggested in 1951 by
295:A protein usually undergoes
7:
3930:Hydrogen–deuterium exchange
3751:Protein structural analysis
2720:10.1529/biophysj.107.118851
2459:Jaenicke R (January 1990).
1277:
1192:structure based drug design
1160:Protein structure databases
845:, which is responsible for
614:
454:Protein secondary structure
314:Levels of protein structure
247:three-dimensional structure
10:
4240:
3287:Protein structural domains
3006:PLOS Computational Biology
1840:Bu Z, Callaway DJ (2011).
1246:
1166:protein structure database
1113:nuclear magnetic resonance
1040:
1010:
798:
645:intragenic complementation
568:
503:Protein tertiary structure
500:
451:
333:
288:molecules assemble into a
144:(which is interactive) of
4195:Nucleic acid double helix
4147:
4094:
4041:
3985:
3964:
3948:
3935:Site-directed mutagenesis
3922:
3891:
3860:
3819:
3793:
3757:
3420:
3300:
3274:
3233:
3126:10.1016/j.sbi.2008.02.004
2859:10.1007/s12033-010-9372-4
2354:10.1016/j.sbi.2010.10.008
2319:10.1016/j.jmb.2005.08.074
2166:10.1016/j.bpj.2013.12.046
2109:10.1016/j.str.2010.01.020
2080:Protein Ensemble Database
1993:10.1007/s00418-008-0416-9
1699:10.1093/genetics/51.6.987
1608:10.1016/j.jmb.2008.11.028
1174:experimentally determined
939:Protein Ensemble Database
581:non-covalent interactions
541:are locked into place by
336:Protein primary structure
227:non-covalent interactions
3780:Electron crystallography
2048:10.3389/fmolb.2015.00045
1942:Voet D, Voet JG (2011).
1229:horizontal gene transfer
1137:Vibrational spectroscopy
1117:cryo-electron microscopy
1091:have been determined by
919:Conformational ensembles
753:supersecondary structure
747:Supersecondary structure
527:hydrophobic interactions
410:tandem mass spectrometry
3899:Fluorescence anisotropy
3861:Translational diffusion
3852:Fluorescence anisotropy
3166:29 October 2018 at the
2847:Molecular Biotechnology
2416:The Biochemical Journal
2224:10.1073/pnas.1419528112
1650:10.1126/science.abc7151
1406:The Biochemical Journal
1099:in the protein, in the
1051:between the folded and
887:protein domain dynamics
835:multi-protein complexes
787:. A related concept is
663:, which is involved in
392:, which is read by the
360:are referred to as the
4035:Biomolecular structure
3065:Nucleic Acids Research
2486:10.1098/rstb.1990.0030
1357:Nucleic Acids Research
1294:Nucleic acid structure
1284:Biomolecular structure
1168:is a database that is
1084:
1076:
1049:free energy difference
897:
879:mobile protein domains
827:conformational changes
668:
516:one or several domains
449:
356:. The two ends of the
326:
308:conformational changes
207:condensation reactions
163:
139:
3994:Quaternary structure→
3956:Equilibrium unfolding
3940:Chemical modification
3909:Dielectric relaxation
3770:X-ray crystallography
3350:Photoreceptor protein
3108:Zhang Y (June 2008).
1519:10.1073/pnas.37.4.205
1225:protein superfamilies
1188:computational biology
1182:information, whereas
1179:x-ray crystallography
1093:X-ray crystallography
1082:
1071:
1043:Equilibrium unfolding
895:
807:conformational states
658:
447:
364:(C-terminus) and the
324:
255:X-ray crystallography
137:
132:
3892:Rotational diffusion
3241:Protein biosynthesis
3192:at Wikimedia Commons
1253:The generation of a
1057:Protein denaturation
815:allosteric signaling
565:Quaternary structure
531:hydrophobic residues
396:in a process called
354:protein biosynthesis
239:Van der Waals forces
45:improve this article
4165:Protein engineering
3989:←Tertiary structure
3018:2009PLSCB...5E0331P
2769:2012PLoSO...746147M
2712:2008BpJ....94.1818J
2700:Biophysical Journal
2530:1958Natur.181..662K
2477:1990RSPTB.326..535J
2215:2015PNAS..112.3409K
2158:2014BpJ...106..865D
2146:Biophysical Journal
1911:10.1038/nature08615
1903:2009Natur.462..669F
1510:1951PNAS...37..205P
1463:1959Sci...129.1340G
1457:(3359): 1340–1344.
1172:around the various
1122:virus coat proteins
1103:state, and thereby
1025:and folds into its
902:tertiary structures
837:. Examples include
831:biological machines
757:secondary structure
713:genetic engineering
707:-binding domain of
639:by nearby adjacent
605:symmetry operations
491:supersecondary unit
459:Secondary structure
440:Secondary structure
280:can be formed from
60:"Protein structure"
3904:Flow birefringence
3832:Circular dichroism
3190:Protein structures
3077:10.1093/nar/gkq366
1829:on 5 January 2013.
1565:10.1002/prot.21473
1369:10.1093/nar/gki615
1184:sequence databases
1133:circular dichroism
1085:
1077:
991:. You can help by
915:tertiary structure
911:tertiary structure
898:
669:
520:globular structure
514:). It may include
508:Tertiary structure
497:Tertiary structure
450:
327:
300:structural changes
251:structural biology
235:ionic interactions
164:
140:
4224:Protein structure
4208:Protein Structure
4203:
4202:
4001:
4000:
3977:Molecular docking
3806:Mass spectrometry
3801:Fiber diffraction
3794:Medium resolution
3717:
3716:
3380:
3379:
3282:Protein structure
3256:Protein targeting
3188:Media related to
2938:on 26 April 2012.
2818:(11): 1163–1179.
2663:10.1021/ja2114135
2657:(11): 5032–5035.
2570:. 1 October 2022.
2524:(4610): 662–666.
2471:(1237): 535–553.
2428:10.1042/bj1280737
2393:978-0-8153-3218-3
2274:10.1021/bi5009326
2268:(46): 7170–7183.
2209:(11): 3409–3414.
1897:(7273): 669–673.
1418:10.1042/bj0490463
1363:(10): 3390–3400.
1337:978-1-305-68645-8
1268:homology modeling
1204:topological class
1154:molecular dynamic
1089:Protein Data Bank
1037:Protein stability
1009:
1008:
689:structural domain
683:Structural domain
512:polypeptide chain
483:Ramachandran plot
406:Edman degradation
362:carboxyl terminus
358:polypeptide chain
342:primary structure
330:Primary structure
278:protein complexes
167:Protein structure
146:protein structure
121:
120:
113:
95:
4231:
4190:Structural motif
4028:
4021:
4014:
4005:
4004:
3878:Light scattering
3744:
3737:
3730:
3721:
3720:
3407:
3400:
3393:
3384:
3383:
3360:Phycobiliprotein
3318:Globular protein
3313:Membrane protein
3308:List of proteins
3220:
3213:
3206:
3197:
3196:
3187:
3148:
3147:
3137:
3105:
3099:
3098:
3088:
3056:
3050:
3049:
3039:
3029:
2997:
2988:
2987:
2977:
2968:(8): 1093–1108.
2946:
2940:
2939:
2937:
2931:. Archived from
2906:
2885:
2879:
2878:
2842:
2836:
2835:
2807:
2801:
2800:
2790:
2780:
2748:
2742:
2741:
2731:
2706:(5): 1818–1825.
2691:
2685:
2684:
2674:
2648:
2639:
2633:
2632:
2626:
2622:
2620:
2612:
2578:
2572:
2571:
2568:"PDB Statistics"
2564:
2558:
2557:
2538:10.1038/181662a0
2513:
2507:
2506:
2488:
2456:
2450:
2449:
2439:
2404:
2398:
2397:
2372:
2366:
2365:
2337:
2331:
2330:
2313:(5): 1118–1128.
2302:
2296:
2295:
2285:
2253:
2247:
2246:
2236:
2226:
2194:
2188:
2187:
2177:
2137:
2131:
2130:
2120:
2088:
2082:
2077:
2071:
2070:
2060:
2050:
2026:
2015:
2014:
2004:
1972:
1966:
1965:
1939:
1933:
1932:
1922:
1882:
1876:
1875:
1837:
1831:
1830:
1825:. Archived from
1808:
1776:
1770:
1769:
1759:
1748:10.1002/pro.2664
1727:
1721:
1720:
1710:
1678:
1672:
1671:
1661:
1629:
1620:
1619:
1591:
1585:
1584:
1548:
1542:
1541:
1531:
1521:
1489:
1483:
1482:
1446:
1440:
1439:
1429:
1397:
1391:
1390:
1380:
1348:
1342:
1341:
1321:
1255:protein sequence
1237:circuit topology
1031:Anfinsen's dogma
1004:
1001:
983:
976:
875:Flexible linkers
823:Protein dynamics
819:enzyme catalysis
801:Protein dynamics
789:protein topology
761:helix-turn-helix
529:, the burial of
426:phosphorylations
402:Frederick Sanger
282:protein subunits
259:NMR spectroscopy
231:hydrogen bonding
197:, which are the
161:
152:as an example. (
136:
125:
116:
109:
105:
102:
96:
94:
53:
29:
21:
4239:
4238:
4234:
4233:
4232:
4230:
4229:
4228:
4214:
4213:
4204:
4199:
4143:
4090:
4037:
4032:
4002:
3997:
3996:
3991:
3981:
3960:
3944:
3918:
3887:
3856:
3815:
3789:
3758:High resolution
3753:
3748:
3718:
3713:
3416:
3414:Protein domains
3411:
3381:
3376:
3340:Fibrous protein
3296:
3270:
3266:Protein methods
3251:Protein folding
3229:
3224:
3180:
3168:Wayback Machine
3157:
3155:Further reading
3152:
3151:
3106:
3102:
3057:
3053:
3012:(3): e1000331.
2998:
2991:
2956:(August 1997).
2947:
2943:
2935:
2904:
2886:
2882:
2843:
2839:
2808:
2804:
2749:
2745:
2692:
2688:
2646:
2640:
2636:
2624:
2623:
2614:
2613:
2601:
2579:
2575:
2566:
2565:
2561:
2514:
2510:
2457:
2453:
2405:
2401:
2394:
2373:
2369:
2338:
2334:
2303:
2299:
2254:
2250:
2195:
2191:
2138:
2134:
2089:
2085:
2078:
2074:
2027:
2018:
1973:
1969:
1954:
1940:
1936:
1883:
1879:
1864:
1838:
1834:
1777:
1773:
1736:Protein Science
1728:
1724:
1693:(6): 987–1002.
1679:
1675:
1644:(6524): 57–64.
1630:
1623:
1592:
1588:
1549:
1545:
1490:
1486:
1447:
1443:
1398:
1394:
1349:
1345:
1338:
1322:
1318:
1313:
1280:
1251:
1245:
1200:
1162:
1066:
1045:
1039:
1015:
1013:Protein folding
1005:
999:
996:
989:needs expansion
974:
972:Protein folding
803:
797:
769:
749:
741:sequence motifs
733:
685:
653:
617:
573:
567:
551:disulfide bonds
505:
499:
456:
442:
371:
338:
332:
316:
153:
131:
123:
117:
106:
100:
97:
54:
52:
42:
30:
17:
12:
11:
5:
4237:
4227:
4226:
4212:
4211:
4210:drugdesign.org
4201:
4200:
4198:
4197:
4192:
4187:
4182:
4177:
4172:
4167:
4162:
4160:Protein domain
4157:
4151:
4149:
4145:
4144:
4142:
4141:
4139:Thermodynamics
4136:
4131:
4126:
4121:
4116:
4111:
4106:
4100:
4098:
4092:
4091:
4089:
4088:
4086:Thermodynamics
4083:
4078:
4073:
4068:
4063:
4058:
4053:
4047:
4045:
4039:
4038:
4031:
4030:
4023:
4016:
4008:
3999:
3998:
3992:
3987:
3986:
3983:
3982:
3980:
3979:
3974:
3968:
3966:
3962:
3961:
3959:
3958:
3952:
3950:
3946:
3945:
3943:
3942:
3937:
3932:
3926:
3924:
3920:
3919:
3917:
3916:
3911:
3906:
3901:
3895:
3893:
3889:
3888:
3886:
3885:
3880:
3875:
3870:
3864:
3862:
3858:
3857:
3855:
3854:
3849:
3844:
3839:
3834:
3829:
3823:
3821:
3817:
3816:
3814:
3813:
3808:
3803:
3797:
3795:
3791:
3790:
3788:
3787:
3782:
3777:
3772:
3767:
3761:
3759:
3755:
3754:
3747:
3746:
3739:
3732:
3724:
3715:
3714:
3712:
3711:
3706:
3701:
3696:
3691:
3686:
3681:
3676:
3671:
3666:
3661:
3656:
3655:
3654:
3644:
3639:
3634:
3629:
3624:
3619:
3614:
3609:
3604:
3599:
3594:
3589:
3584:
3579:
3574:
3569:
3568:
3567:
3562:
3557:
3552:
3542:
3537:
3532:
3527:
3522:
3517:
3512:
3507:
3502:
3497:
3492:
3487:
3482:
3477:
3472:
3467:
3462:
3457:
3452:
3447:
3442:
3437:
3432:
3427:
3421:
3418:
3417:
3410:
3409:
3402:
3395:
3387:
3378:
3377:
3375:
3374:
3373:
3372:
3367:
3362:
3352:
3347:
3342:
3337:
3336:
3335:
3330:
3325:
3315:
3310:
3304:
3302:
3298:
3297:
3295:
3294:
3289:
3284:
3278:
3276:
3272:
3271:
3269:
3268:
3263:
3258:
3253:
3248:
3243:
3237:
3235:
3231:
3230:
3223:
3222:
3215:
3208:
3200:
3194:
3193:
3179:
3178:External links
3176:
3175:
3174:
3156:
3153:
3150:
3149:
3120:(3): 342–348.
3100:
3051:
2989:
2941:
2915:(4): 536–540.
2900:(April 1995).
2880:
2853:(2): 183–198.
2837:
2802:
2763:(10): e46147.
2743:
2686:
2634:
2625:|journal=
2599:
2573:
2559:
2508:
2451:
2422:(4): 737–749.
2399:
2392:
2367:
2332:
2297:
2248:
2189:
2152:(4): 865–874.
2132:
2103:(4): 494–506.
2083:
2072:
2016:
1987:(6): 687–693.
1967:
1952:
1934:
1877:
1862:
1832:
1791:(4): 408–414.
1771:
1742:(5): 874–882.
1722:
1673:
1621:
1602:(3): 726–732.
1586:
1559:(4): 915–921.
1543:
1504:(4): 205–211.
1484:
1441:
1412:(4): 463–481.
1392:
1343:
1336:
1315:
1314:
1312:
1309:
1308:
1307:
1304:Ribbon diagram
1301:
1296:
1291:
1289:Gene structure
1286:
1279:
1276:
1272:protein family
1247:Main article:
1244:
1241:
1199:
1196:
1161:
1158:
1065:
1062:
1041:Main article:
1038:
1035:
1011:Main article:
1007:
1006:
986:
984:
973:
970:
963:Beta-synuclein
839:motor proteins
799:Main article:
796:
793:
768:
765:
748:
745:
732:
729:
684:
681:
652:
649:
616:
613:
569:Main article:
566:
563:
539:protein domain
501:Main article:
498:
495:
479:hydrogen bonds
452:Main article:
441:
438:
430:glycosylations
418:water molecule
369:
366:amino terminus
334:Main article:
331:
328:
315:
312:
211:water molecule
119:
118:
33:
31:
24:
15:
9:
6:
4:
3:
2:
4236:
4225:
4222:
4221:
4219:
4209:
4206:
4205:
4196:
4193:
4191:
4188:
4186:
4183:
4181:
4178:
4176:
4173:
4171:
4168:
4166:
4163:
4161:
4158:
4156:
4153:
4152:
4150:
4146:
4140:
4137:
4135:
4132:
4130:
4127:
4125:
4124:Determination
4122:
4120:
4117:
4115:
4112:
4110:
4107:
4105:
4102:
4101:
4099:
4097:
4093:
4087:
4084:
4082:
4079:
4077:
4074:
4072:
4071:Determination
4069:
4067:
4064:
4062:
4059:
4057:
4054:
4052:
4049:
4048:
4046:
4044:
4040:
4036:
4029:
4024:
4022:
4017:
4015:
4010:
4009:
4006:
3995:
3990:
3984:
3978:
3975:
3973:
3970:
3969:
3967:
3965:Computational
3963:
3957:
3954:
3953:
3951:
3949:Thermodynamic
3947:
3941:
3938:
3936:
3933:
3931:
3928:
3927:
3925:
3921:
3915:
3912:
3910:
3907:
3905:
3902:
3900:
3897:
3896:
3894:
3890:
3884:
3881:
3879:
3876:
3874:
3871:
3869:
3866:
3865:
3863:
3859:
3853:
3850:
3848:
3845:
3843:
3840:
3838:
3835:
3833:
3830:
3828:
3825:
3824:
3822:
3820:Spectroscopic
3818:
3812:
3809:
3807:
3804:
3802:
3799:
3798:
3796:
3792:
3786:
3783:
3781:
3778:
3776:
3773:
3771:
3768:
3766:
3763:
3762:
3760:
3756:
3752:
3745:
3740:
3738:
3733:
3731:
3726:
3725:
3722:
3710:
3707:
3705:
3702:
3700:
3697:
3695:
3692:
3690:
3687:
3685:
3682:
3680:
3677:
3675:
3672:
3670:
3667:
3665:
3662:
3660:
3657:
3653:
3650:
3649:
3648:
3645:
3643:
3640:
3638:
3635:
3633:
3630:
3628:
3625:
3623:
3620:
3618:
3615:
3613:
3610:
3608:
3605:
3603:
3600:
3598:
3595:
3593:
3590:
3588:
3585:
3583:
3580:
3578:
3575:
3573:
3570:
3566:
3563:
3561:
3558:
3556:
3553:
3551:
3548:
3547:
3546:
3543:
3541:
3538:
3536:
3533:
3531:
3528:
3526:
3523:
3521:
3518:
3516:
3513:
3511:
3508:
3506:
3503:
3501:
3498:
3496:
3493:
3491:
3488:
3486:
3483:
3481:
3478:
3476:
3473:
3471:
3468:
3466:
3463:
3461:
3458:
3456:
3453:
3451:
3448:
3446:
3443:
3441:
3438:
3436:
3433:
3431:
3428:
3426:
3423:
3422:
3419:
3415:
3408:
3403:
3401:
3396:
3394:
3389:
3388:
3385:
3371:
3368:
3366:
3363:
3361:
3358:
3357:
3356:
3353:
3351:
3348:
3346:
3345:Chromoprotein
3343:
3341:
3338:
3334:
3331:
3329:
3326:
3324:
3321:
3320:
3319:
3316:
3314:
3311:
3309:
3306:
3305:
3303:
3299:
3293:
3290:
3288:
3285:
3283:
3280:
3279:
3277:
3273:
3267:
3264:
3262:
3259:
3257:
3254:
3252:
3249:
3247:
3244:
3242:
3239:
3238:
3236:
3232:
3228:
3221:
3216:
3214:
3209:
3207:
3202:
3201:
3198:
3191:
3186:
3182:
3181:
3173:
3169:
3165:
3162:
3159:
3158:
3145:
3141:
3136:
3131:
3127:
3123:
3119:
3115:
3111:
3104:
3096:
3092:
3087:
3082:
3078:
3074:
3070:
3066:
3062:
3055:
3047:
3043:
3038:
3033:
3028:
3023:
3019:
3015:
3011:
3007:
3003:
2996:
2994:
2985:
2981:
2976:
2971:
2967:
2963:
2959:
2955:
2951:
2945:
2934:
2930:
2926:
2922:
2918:
2914:
2910:
2903:
2899:
2895:
2891:
2884:
2876:
2872:
2868:
2864:
2860:
2856:
2852:
2848:
2841:
2833:
2829:
2825:
2821:
2817:
2813:
2806:
2798:
2794:
2789:
2784:
2779:
2774:
2770:
2766:
2762:
2758:
2754:
2747:
2739:
2735:
2730:
2725:
2721:
2717:
2713:
2709:
2705:
2701:
2697:
2690:
2682:
2678:
2673:
2668:
2664:
2660:
2656:
2652:
2645:
2638:
2630:
2618:
2610:
2606:
2602:
2600:9780120342389
2596:
2592:
2588:
2584:
2577:
2569:
2563:
2555:
2551:
2547:
2543:
2539:
2535:
2531:
2527:
2523:
2519:
2512:
2504:
2500:
2496:
2492:
2487:
2482:
2478:
2474:
2470:
2466:
2462:
2455:
2447:
2443:
2438:
2433:
2429:
2425:
2421:
2417:
2413:
2410:(July 1972).
2409:
2403:
2395:
2389:
2385:
2381:
2377:
2371:
2363:
2359:
2355:
2351:
2347:
2343:
2336:
2328:
2324:
2320:
2316:
2312:
2308:
2301:
2293:
2289:
2284:
2279:
2275:
2271:
2267:
2263:
2259:
2252:
2244:
2240:
2235:
2230:
2225:
2220:
2216:
2212:
2208:
2204:
2200:
2193:
2185:
2181:
2176:
2171:
2167:
2163:
2159:
2155:
2151:
2147:
2143:
2136:
2128:
2124:
2119:
2114:
2110:
2106:
2102:
2098:
2094:
2087:
2081:
2076:
2068:
2064:
2059:
2054:
2049:
2044:
2040:
2036:
2032:
2025:
2023:
2021:
2012:
2008:
2003:
1998:
1994:
1990:
1986:
1982:
1978:
1971:
1963:
1959:
1955:
1953:9780470570951
1949:
1945:
1938:
1930:
1926:
1921:
1916:
1912:
1908:
1904:
1900:
1896:
1892:
1888:
1881:
1873:
1869:
1865:
1863:9780123812629
1859:
1855:
1851:
1847:
1843:
1836:
1828:
1824:
1820:
1816:
1812:
1807:
1806:2027.42/34969
1802:
1798:
1794:
1790:
1786:
1782:
1775:
1767:
1763:
1758:
1753:
1749:
1745:
1741:
1737:
1733:
1726:
1718:
1714:
1709:
1704:
1700:
1696:
1692:
1688:
1684:
1677:
1669:
1665:
1660:
1655:
1651:
1647:
1643:
1639:
1635:
1628:
1626:
1617:
1613:
1609:
1605:
1601:
1597:
1590:
1582:
1578:
1574:
1570:
1566:
1562:
1558:
1554:
1547:
1539:
1535:
1530:
1525:
1520:
1515:
1511:
1507:
1503:
1499:
1495:
1488:
1480:
1476:
1472:
1468:
1464:
1460:
1456:
1452:
1445:
1437:
1433:
1428:
1423:
1419:
1415:
1411:
1407:
1403:
1396:
1388:
1384:
1379:
1374:
1370:
1366:
1362:
1358:
1354:
1347:
1339:
1333:
1329:
1328:
1320:
1316:
1305:
1302:
1300:
1297:
1295:
1292:
1290:
1287:
1285:
1282:
1281:
1275:
1273:
1269:
1265:
1261:
1256:
1250:
1240:
1238:
1234:
1230:
1226:
1222:
1217:
1213:
1209:
1205:
1195:
1193:
1189:
1185:
1180:
1175:
1171:
1167:
1157:
1155:
1151:
1147:
1142:
1138:
1134:
1129:
1127:
1123:
1118:
1114:
1110:
1106:
1102:
1098:
1094:
1090:
1081:
1075:
1070:
1061:
1058:
1054:
1050:
1044:
1034:
1032:
1028:
1024:
1020:
1014:
1003:
994:
990:
987:This section
985:
982:
978:
977:
969:
968:
964:
960:
956:
952:
948:
943:
940:
936:
931:
926:
924:
920:
916:
912:
908:
903:
894:
890:
888:
884:
880:
876:
872:
868:
864:
860:
856:
852:
849:contraction,
848:
844:
840:
836:
832:
828:
824:
820:
816:
812:
808:
802:
792:
790:
786:
782:
781:Rossmann fold
778:
774:
764:
762:
758:
754:
744:
742:
738:
728:
726:
722:
718:
714:
710:
706:
702:
698:
694:
690:
680:
678:
674:
666:
662:
657:
648:
646:
642:
638:
634:
630:
626:
622:
612:
610:
606:
602:
598:
594:
590:
586:
582:
578:
572:
562:
561:environment.
560:
556:
552:
548:
544:
540:
536:
532:
528:
525:
521:
517:
513:
509:
504:
494:
492:
488:
484:
480:
476:
475:Linus Pauling
472:
468:
464:
460:
455:
446:
437:
435:
431:
427:
423:
419:
415:
411:
407:
403:
399:
395:
391:
387:
383:
379:
375:
367:
363:
359:
355:
351:
350:peptide bonds
347:
343:
337:
323:
319:
311:
309:
305:
304:conformations
301:
298:
293:
291:
290:microfilament
287:
283:
279:
275:
274:nanoparticles
270:
268:
264:
260:
256:
252:
248:
244:
240:
236:
232:
228:
224:
220:
216:
212:
208:
204:
200:
196:
192:
188:
184:
180:
176:
172:
168:
160:
156:
151:
147:
143:
115:
112:
104:
93:
90:
86:
83:
79:
76:
72:
69:
65:
62: –
61:
57:
56:Find sources:
50:
46:
40:
39:
34:This article
32:
28:
23:
22:
19:
4175:Nucleic acid
4096:Nucleic acid
4042:
3847:Fluorescence
3750:
3281:
3117:
3113:
3103:
3068:
3064:
3054:
3009:
3005:
2965:
2961:
2944:
2933:the original
2912:
2908:
2883:
2850:
2846:
2840:
2815:
2811:
2805:
2760:
2756:
2746:
2703:
2699:
2689:
2654:
2650:
2637:
2582:
2576:
2562:
2521:
2517:
2511:
2468:
2464:
2454:
2419:
2415:
2402:
2383:
2370:
2348:(1): 25–31.
2345:
2341:
2335:
2310:
2306:
2300:
2265:
2262:Biochemistry
2261:
2251:
2206:
2202:
2192:
2149:
2145:
2135:
2100:
2096:
2086:
2075:
2038:
2034:
2013:. 1432-119X.
1984:
1980:
1970:
1944:Biochemistry
1943:
1937:
1894:
1890:
1880:
1845:
1835:
1827:the original
1788:
1784:
1774:
1739:
1735:
1725:
1690:
1686:
1676:
1641:
1637:
1599:
1595:
1589:
1556:
1552:
1546:
1501:
1497:
1487:
1454:
1450:
1444:
1409:
1405:
1395:
1360:
1356:
1346:
1326:
1319:
1259:
1252:
1210:origin. The
1208:evolutionary
1206:or a common
1201:
1163:
1130:
1101:crystallized
1086:
1046:
1027:native state
1021:mostly as a
1016:
997:
993:adding to it
988:
944:
927:
899:
867:motile cilia
859:microtubules
804:
773:helix bundle
770:
767:Protein fold
750:
734:
686:
670:
618:
574:
547:salt bridges
542:
524:non-specific
523:
506:
457:
414:genetic code
339:
317:
294:
271:
219:peptide bond
202:
191:polypeptides
166:
165:
145:
142:This diagram
107:
98:
88:
81:
74:
67:
55:
43:Please help
38:verification
35:
18:
3709:zinc finger
3365:Phytochrome
3355:Biliprotein
2954:Thornton JM
2888:Murzin AG,
2408:Anfinsen CB
1233:Knot theory
1146:proteolysis
1023:random coil
723:domain and
701:gene family
621:polypeptide
487:random coil
398:translation
386:transcribed
378:nucleotides
346:amino acids
243:hydrophobic
195:amino acids
4170:Proteasome
4129:Prediction
4119:Quaternary
4076:Prediction
4066:Quaternary
3842:Absorbance
3292:Proteasome
3275:Structures
2890:Brenner SE
1311:References
1000:April 2019
877:allow the
841:, such as
811:nanoscales
737:structural
709:calmodulin
677:eukaryotic
609:hemoglobin
297:reversible
229:, such as
175:amino acid
71:newspapers
4109:Secondary
4056:Secondary
3597:EcoEI_R_C
3370:Lipocalin
3234:Processes
2962:Structure
2950:Orengo CA
2898:Chothia C
2894:Hubbard T
2627:ignored (
2617:cite book
2376:Alberts B
2097:Structure
1962:690489261
1264:Threading
1260:Ab initio
1097:electrons
883:allostery
725:C2 domain
661:PH domain
641:ribosomes
585:multimers
4218:Category
4148:See also
4114:Tertiary
4061:Tertiary
3923:Chemical
3323:Globulin
3261:Proteome
3227:Proteins
3164:Archived
3144:18436442
3095:20457744
3046:19325884
2875:45184564
2867:21225378
2832:28637405
2797:23056252
2757:PLOS ONE
2738:17981904
2681:22356513
2546:13517261
2362:21111607
2327:16214166
2292:25389903
2243:25737554
2184:24559989
2127:20399186
2067:26301226
2011:18365235
1929:19956261
1872:21570668
1815:10382668
1785:Proteins
1766:25694109
1717:14337770
1687:Genetics
1668:33384371
1616:19059267
1581:29904865
1573:17557333
1553:Proteins
1538:14816373
1479:13658959
1436:14886310
1387:15951512
1299:PCRPi-DB
1278:See also
1221:homology
1190:such as
1128:fibers.
1053:unfolded
1019:ribosome
935:ensemble
930:ensemble
928:Protein
871:flagella
777:β-barrel
633:oligomer
629:multimer
615:Homomers
601:pentamer
597:tetramer
577:multimer
559:reducing
543:specific
471:β-sheets
467:β-strand
465:and the
424:such as
394:ribosome
215:reaction
199:monomers
187:polymers
183:Proteins
179:molecule
101:May 2018
4155:Protein
4104:Primary
4051:Primary
4043:Protein
3627:Kringle
3520:CGI-121
3490:BTB/POZ
3333:Albumin
3328:Edestin
3135:2680823
3086:2896194
3037:2654728
3014:Bibcode
2984:9309224
2929:7723011
2788:3463568
2765:Bibcode
2729:2242754
2708:Bibcode
2609:3541539
2554:4162786
2526:Bibcode
2503:1969647
2495:2398703
2473:Bibcode
2446:4565129
2437:1173893
2283:4245978
2234:4371970
2211:Bibcode
2175:3944474
2154:Bibcode
2118:2924144
2058:4525029
2002:2386530
1920:2805857
1899:Bibcode
1823:7147867
1757:4420535
1708:1210828
1659:7613021
1638:Science
1529:1063337
1506:Bibcode
1459:Bibcode
1451:Science
1427:1197535
1378:1150220
1170:modeled
1126:amyloid
955:p15 PAF
855:nucleus
851:kinesin
717:chimera
705:calcium
699:or one
667:binding
625:homomer
555:cytosol
463:α-helix
434:insulin
223:peptide
203:residue
177:-chain
169:is the
85:scholar
4134:Design
4081:Design
3142:
3132:
3093:
3083:
3044:
3034:
2982:
2927:
2873:
2865:
2830:
2795:
2785:
2736:
2726:
2679:
2607:
2597:
2552:
2544:
2518:Nature
2501:
2493:
2444:
2434:
2390:
2360:
2325:
2290:
2280:
2241:
2231:
2182:
2172:
2125:
2115:
2065:
2055:
2041:: 45.
2009:
1999:
1960:
1950:
1927:
1917:
1891:Nature
1870:
1860:
1821:
1813:
1764:
1754:
1715:
1705:
1666:
1656:
1614:
1579:
1571:
1536:
1526:
1477:
1434:
1424:
1385:
1375:
1334:
863:dynein
861:, and
857:along
847:muscle
843:myosin
673:motifs
593:trimer
241:, and
173:in an
87:
80:
73:
66:
58:
3642:NACHT
3565:Pyrin
3545:Death
3510:Cache
3445:ADF-H
3301:Types
2936:(PDF)
2905:(PDF)
2871:S2CID
2647:(PDF)
2550:S2CID
2491:JSTOR
1819:S2CID
1577:S2CID
1109:atoms
1105:infer
693:folds
589:dimer
535:water
533:from
388:into
286:actin
148:uses
92:JSTOR
78:books
3811:SAXS
3694:WD40
3689:TRIO
3622:HEAT
3617:FYVE
3612:FGGY
3607:ENTH
3587:DHR2
3582:DHR1
3577:DHHC
3560:CARD
3540:CVHN
3495:BZIP
3470:BESS
3455:ARID
3450:ANTH
3435:ACDC
3140:PMID
3091:PMID
3042:PMID
2980:PMID
2925:PMID
2863:PMID
2828:PMID
2793:PMID
2734:PMID
2677:PMID
2629:help
2605:PMID
2595:ISBN
2542:PMID
2499:PMID
2442:PMID
2388:ISBN
2358:PMID
2323:PMID
2288:PMID
2239:PMID
2180:PMID
2123:PMID
2063:PMID
2007:PMID
1958:OCLC
1948:ISBN
1925:PMID
1868:PMID
1858:ISBN
1811:PMID
1762:PMID
1713:PMID
1664:PMID
1612:PMID
1569:PMID
1534:PMID
1475:PMID
1432:PMID
1383:PMID
1332:ISBN
1266:and
1235:and
1216:CATH
1214:and
1124:and
965:and
959:MKK7
951:Cdc4
947:Sic1
889:. "
885:via
869:and
825:and
817:and
739:and
735:The
697:gene
637:mRNA
428:and
390:mRNA
374:gene
340:The
265:and
213:per
185:are
159:1AXC
150:PCNA
64:news
4185:RNA
4180:DNA
3914:NMR
3883:NMR
3827:NMR
3785:EPR
3775:NMR
3704:YTH
3684:SUN
3679:SH3
3674:SH2
3659:PDZ
3652:LOV
3647:PAS
3637:LRR
3632:LIM
3602:EF1
3572:DEP
3555:DED
3535:CUT
3530:CUB
3525:CRM
3515:CBS
3485:BPS
3480:BMC
3475:BIR
3465:BEN
3460:BAR
3440:ACT
3430:ABM
3172:NIH
3170:at
3130:PMC
3122:doi
3081:PMC
3073:doi
3032:PMC
3022:doi
2970:doi
2917:doi
2913:247
2855:doi
2820:doi
2783:PMC
2773:doi
2724:PMC
2716:doi
2667:hdl
2659:doi
2655:134
2587:doi
2534:doi
2522:181
2481:doi
2469:326
2432:PMC
2424:doi
2420:128
2350:doi
2315:doi
2311:353
2278:PMC
2270:doi
2229:PMC
2219:doi
2207:112
2170:PMC
2162:doi
2150:106
2113:PMC
2105:doi
2053:PMC
2043:doi
1997:PMC
1989:doi
1985:129
1915:PMC
1907:doi
1895:462
1850:doi
1801:hdl
1793:doi
1752:PMC
1744:doi
1703:PMC
1695:doi
1654:PMC
1646:doi
1642:371
1604:doi
1600:385
1561:doi
1524:PMC
1514:doi
1467:doi
1455:129
1422:PMC
1414:doi
1373:PMC
1365:doi
1074:PDB
1033:).
995:.
967:P27
821:.
631:or
493:".
469:or
408:or
384:is
382:DNA
380:in
155:PDB
47:by
4220::
3699:X8
3669:PX
3664:PH
3592:DM
3550:DD
3505:C2
3500:C1
3425:3H
3138:.
3128:.
3118:18
3116:.
3112:.
3089:.
3079:.
3069:38
3067:.
3063:.
3040:.
3030:.
3020:.
3008:.
3004:.
2992:^
2978:.
2964:.
2960:.
2923:.
2911:.
2907:.
2896:,
2892:,
2869:.
2861:.
2851:48
2849:.
2826:.
2816:18
2814:.
2791:.
2781:.
2771:.
2759:.
2755:.
2732:.
2722:.
2714:.
2704:94
2702:.
2698:.
2675:.
2665:.
2653:.
2649:.
2621::
2619:}}
2615:{{
2603:.
2593:.
2548:.
2540:.
2532:.
2520:.
2497:.
2489:.
2479:.
2467:.
2463:.
2440:.
2430:.
2418:.
2414:.
2382:.
2356:.
2346:21
2344:.
2321:.
2309:.
2286:.
2276:.
2266:53
2264:.
2260:.
2237:.
2227:.
2217:.
2205:.
2201:.
2178:.
2168:.
2160:.
2148:.
2144:.
2121:.
2111:.
2101:18
2099:.
2095:.
2061:.
2051:.
2037:.
2033:.
2019:^
2005:.
1995:.
1983:.
1979:.
1956:.
1923:.
1913:.
1905:.
1893:.
1889:.
1866:.
1856:.
1844:.
1817:.
1809:.
1799:.
1789:35
1787:.
1783:.
1760:.
1750:.
1740:24
1738:.
1734:.
1711:.
1701:.
1691:51
1689:.
1685:.
1662:.
1652:.
1640:.
1636:.
1624:^
1610:.
1598:.
1575:.
1567:.
1557:68
1555:.
1532:.
1522:.
1512:.
1502:37
1500:.
1496:.
1473:.
1465:.
1453:.
1430:.
1420:.
1410:49
1408:.
1404:.
1381:.
1371:.
1361:33
1359:.
1355:.
1274:.
1164:A
1135:.
961:,
957:,
953:,
925:.
917:.
791:.
779:,
775:,
687:A
627:,
611:.
310:.
292:.
261:,
257:,
237:,
233:,
181:.
162:)
157::
4027:e
4020:t
4013:v
3743:e
3736:t
3729:v
3406:e
3399:t
3392:v
3219:e
3212:t
3205:v
3146:.
3124::
3097:.
3075::
3048:.
3024::
3016::
3010:5
2986:.
2972::
2966:5
2919::
2877:.
2857::
2834:.
2822::
2799:.
2775::
2767::
2761:7
2740:.
2718::
2710::
2683:.
2669::
2661::
2631:)
2611:.
2589::
2556:.
2536::
2528::
2505:.
2483::
2475::
2448:.
2426::
2396:.
2364:.
2352::
2329:.
2317::
2294:.
2272::
2245:.
2221::
2213::
2186:.
2164::
2156::
2129:.
2107::
2069:.
2045::
2039:2
1991::
1964:.
1931:.
1909::
1901::
1874:.
1852::
1803::
1795::
1768:.
1746::
1719:.
1697::
1670:.
1648::
1618:.
1606::
1583:.
1563::
1540:.
1516::
1508::
1481:.
1469::
1461::
1438:.
1416::
1389:.
1367::
1340:.
1002:)
998:(
949:/
370:2
114:)
108:(
103:)
99:(
89:·
82:·
75:·
68:·
41:.
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
-en.svg){kind=link}