Blind test of physics-based prediction of protein structures.

Abstract:

:We report here a multiprotein blind test of a computer method to predict native protein structures based solely on an all-atom physics-based force field. We use the AMBER 96 potential function with an implicit (GB/SA) model of solvation, combined with replica-exchange molecular-dynamics simulations. Coarse conformational sampling is performed using the zipping and assembly method (ZAM), an approach that is designed to mimic the putative physical routes of protein folding. ZAM was applied to the folding of six proteins, from 76 to 112 monomers in length, in CASP7, a community-wide blind test of protein structure prediction. Because these predictions have about the same level of accuracy as typical bioinformatics methods, and do not utilize information from databases of known native structures, this work opens up the possibility of predicting the structures of membrane proteins, synthetic peptides, or other foldable polymers, for which there is little prior knowledge of native structures. This approach may also be useful for predicting physical protein folding routes, non-native conformations, and other physical properties from amino acid sequences.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Shell MS,Ozkan SB,Voelz V,Wu GA,Dill KA

doi

10.1016/j.bpj.2008.11.009

subject

Has Abstract

pub_date

2009-02-01 00:00:00

pages

917-24

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(08)00446-3

journal_volume

96

pub_type

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