Protein structures and optimal folding emerging from a geometrical variational principle
Abstract
Novel numerical techniques, validated by an analysis of barnase and chymotrypsin inhibitor, are used to elucidate the paramount role played by the geometry of the protein backbone in steering the folding to the correct native state. It is found that, irrespective of the sequence, the native state of a protein has exceedingly large number of conformations with a given amount of structural overlap compared to other compact artificial backbones; moreover the conformational entropies of unrelated proteins of the same length are nearly equal at any given stage of folding. These results are suggestive of an extremality principle underlying protein evolution, which, in turn, is shown to be associated with the emergence of secondary structures.
Cite
@article{arxiv.cond-mat/9811246,
title = {Protein structures and optimal folding emerging from a geometrical variational principle},
author = {Cristian Micheletti and Jayanth R. Banavar and Amos Maritan and Flavio Seno},
journal= {arXiv preprint arXiv:cond-mat/9811246},
year = {2009}
}
Comments
Revtex, 5 pages, 5 postscript figures