ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
During evolution, the effective interactions between residues in a protein can be adjusted through mutations to allow the protein to fold to its native structure on an adequate time scale. We seek to address the question: Are there some structures that can be better optimized than others? Using exhaustive enumeration of the compact conformations of short proteins confined to simple lattices, we find that the best structures are those that contain contacts rare in random structures, indicating the importance of nonlocal contacts for assisting the folding process. Certain structural motifs such as long β-hairpins, Greek-key motifs, and jelly rolls, commonly found in proteins of known structure, have a high degree of optimizability. Contrary to what might be expected, positive correlations between the various interactions reduce optimizability. The optimization procedure produces a correlated energy landscape, which might assist folding. © 1995 John Wiley & Sons, Inc.
Additional Material:
5 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bip.360360105
