Geometry and symmetry presculpt the free-energy landscape of proteins.
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ABSTRACT:
SUBMITTER: Hoang TX
PROVIDER: S-EPMC419539 | biostudies-other | 2004 May
REPOSITORIES: biostudies-other
Publications
Geometry and symmetry presculpt the free-energy landscape of proteins.
Hoang Trinh Xuan TX Trovato Antonio A Seno Flavio F Banavar Jayanth R JR Maritan Amos A
Proceedings of the National Academy of Sciences of the United States of America 20040517 21
We present a simple physical model that demonstrates that the native-state folds of proteins can emerge on the basis of considerations of geometry and symmetry. We show that the inherent anisotropy of a chain molecule, the geometrical and energetic constraints placed by the hydrogen bonds and sterics, and hydrophobicity are sufficient to yield a free-energy landscape with broad minima even for a homopolymer. These minima correspond to marginally compact structures comprising the menu of folds th ...[more]
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