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National Academy of Sciences, Proceedings of the National Academy of Sciences, 21(101), p. 7960-7964, 2004

DOI: 10.1073/pnas.0402525101

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Geometry and symmetry presculpt the free-energy landscape of proteins

Journal article published in 2004 by Trinh Xuan Hoang ORCID, Antonio Trovato, Flavio Seno, Jayanth R. Banavar, Amos Maritan
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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 that proteins choose from to house their native states in. Our results provide a general framework for understanding the common characteristics of globular proteins.