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Structure. 2007 Jan;15(1):53-63.

All-atom ab initio folding of a diverse set of proteins.

Author information

1
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.

Abstract

Natural proteins fold to a unique, thermodynamically dominant state. Modeling of the folding process and prediction of the native fold of proteins are two major unsolved problems in biophysics. Here, we show successful all-atom ab initio folding of a representative diverse set of proteins by using a minimalist transferable-energy model that consists of two-body atom-atom interactions, hydrogen bonding, and a local sequence-energy term that models sequence-specific chain stiffness. Starting from a random coil, the native-like structure was observed during replica exchange Monte Carlo (REMC) simulation for most proteins regardless of their structural classes; the lowest energy structure was close to native-in the range of 2-6 A root-mean-square deviation (rmsd). Our results demonstrate that the successful folding of a protein chain to its native state is governed by only a few crucial energetic terms.

PMID:
17223532
DOI:
10.1016/j.str.2006.11.010
[Indexed for MEDLINE]
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