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Probing protein fold space with a simplified model.

Abstract:

We probe the stability and near-native energy landscape of protein fold space using powerful conformational sampling methods together with simple reduced models and statistical potentials. Fold space is represented by a set of 280 protein domains spanning all topological classes and having a wide range of lengths (33-300 residues) amino acid composition and number of secondary structural elements. The degrees of freedom are taken as the loop torsion angles. This choice preserves the native se...

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Publisher copy:
10.1016/j.jmb.2007.10.087

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Institution:
University of Oxford
Department:
Oxford, MPLS, Computer Science
Journal:
Journal of molecular biology
Volume:
375
Issue:
4
Pages:
920-933
Publication date:
2008-01-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:6de649e4-926f-4bf2-ad03-508c0168e196
Source identifiers:
375985
Local pid:
pubs:375985

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