Abstract
AbstractDespite the variety of protein sizes, shapes, and backbone configurations found in nature, the design of novel protein folds remains an open problem. Within simple lattice models it has been shown that all structures are not equally suitable for design. Rather, certain structures are distinguished by unusually high designability: the number of amino acid sequences for which they represent the unique lowest energy state; sequences associated with such structures possess both robustness to mutation and thermodynamic stability. Here we report that highly designable backbone conformations also emerge in a realistic off‐lattice model. The highly designable conformations of a chain of 23 amino acids are identified and found to be remarkably insensitive to model parameters. Although some of these conformations correspond closely to known natural protein folds, such as the zinc finger and the helix‐turn‐helix motifs, others do not resemble known folds and may be candidates for novel fold design. Proteins 2002;47:506–512. © 2002 Wiley‐Liss, Inc.
References
38
Referenced
40
10.1074/jbc.272.4.2031
10.1016/S0959-440X(98)80124-3
{'key': 'e_1_2_6_4_2', 'first-page': '197', 'article-title': 'The current state and prospect of de novo protein design', 'volume': '25', 'author': 'Cao AN', 'year': '1998', 'journal-title': 'Prog Biochem Biophys'}
/ Prog Biochem Biophys / The current state and prospect of de novo protein design by Cao AN (1998)10.1016/S1367-5931(98)80006-9
10.1016/S0959-440X(98)80120-6
10.1016/S0958-1669(98)80006-2
10.1016/S1359-0278(98)00021-2
10.1146/annurev.biochem.68.1.779
10.1126/science.282.5393.1462
10.1126/science.271.5247.342
10.1126/science.278.5335.82
10.1006/jmbi.1997.1341
10.1038/357543a0
10.1126/science.273.5275.666
10.1073/pnas.95.9.4987
10.1002/bip.360360105
10.1073/pnas.93.8.3341
10.1016/0079-6107(87)90013-7
10.1073/pnas.92.1.146
10.1063/1.478168
10.1006/jmbi.1995.0311
10.1016/S1093-3263(97)00082-X
{'key': 'e_1_2_6_24_2', 'first-page': '160', 'volume-title': 'Proteins', 'author': 'Creighton TE', 'year': '1993'}
/ Proteins by Creighton TE (1993)10.1021/ma00200a030
10.1021/bi981818o
10.1006/jmbi.1998.1645
10.1038/33808
10.1103/PhysRevLett.81.5237
10.1038/14866
10.1016/S0959-440X(99)80027-X
10.1073/pnas.97.4.1525
10.1103/PhysRevLett.84.3009
10.1038/35011000
10.1006/jmbi.2000.3693
10.1021/bi000200n
10.1016/S0959-440X(00)00170-6
10.1006/jmbi.2000.3622
10.1073/pnas.96.5.1983
Dates
Type | When |
---|---|
Created | 20 years, 10 months ago (Oct. 27, 2004, 7:10 a.m.) |
Deposited | 1 year, 10 months ago (Oct. 16, 2023, 12:10 a.m.) |
Indexed | 2 months, 2 weeks ago (June 16, 2025, 9:07 a.m.) |
Issued | 23 years, 4 months ago (April 19, 2002) |
Published | 23 years, 4 months ago (April 19, 2002) |
Published Online | 23 years, 4 months ago (April 19, 2002) |
Published Print | 23 years, 2 months ago (June 1, 2002) |
@article{Miller_2002, title={Emergence of highly designable protein‐backbone conformations in an off‐lattice model}, volume={47}, ISSN={1097-0134}, url={http://dx.doi.org/10.1002/prot.10107}, DOI={10.1002/prot.10107}, number={4}, journal={Proteins: Structure, Function, and Bioinformatics}, publisher={Wiley}, author={Miller, Jonathan and Zeng, Chen and Wingreen, Ned S. and Tang, Chao}, year={2002}, month=apr, pages={506–512} }