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26 April 2024 |
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Geometry and symmetry presculpt the free-energy landscape of proteins | | Trinh Xuan Hoang
; Antonio Trovato
; Flavio Seno
; Jayanth R. Banavar
; Amos Maritan
; | | Date: |
25 May 2004 | | Journal: | PNAS 101, 7960-7964 (2004) | | Subject: | Biomolecules | q-bio.BM | | Abstract: | We present a simple physical model which 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. | | Source: | arXiv, q-bio.BM/0405019 | | Other source: | [GID 1023341] pnas | | Services: | Forum | Review | PDF | Favorites | |
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