Literature DB >> 19628506

Enhancement of beta-sheet assembly by cooperative hydrogen bonds potential.

Ami Levy-Moonshine1, El-Ad David Amir, Chen Keasar.   

Abstract

MOTIVATION: The roughness of energy landscapes is a major obstacle to protein structure prediction, since it forces conformational searches to spend much time struggling to escape numerous traps. Specifically, beta-sheet formation is prone to stray, since many possible combinations of hydrogen bonds are dead ends in terms of beta-sheet assembly. It has been shown that cooperative terms for backbone hydrogen bonds ease this problem by augmenting hydrogen bond patterns that are consistent with beta sheets. Here, we present a novel cooperative hydrogen-bond term that is both effective in promoting beta sheets and computationally efficient. In addition, the new term is differentiable and operates on all-atom protein models.
RESULTS: Energy optimization of poly-alanine chains under the new term led to significantly more beta-sheet content than optimization under a non-cooperative term. Furthermore, the optimized structure included very few non-native patterns. AVAILABILITY: The new term is implemented within the MESHI package and is freely available at http://cs.bgu.ac.il/ approximately meshi.

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Year:  2009        PMID: 19628506      PMCID: PMC3140807          DOI: 10.1093/bioinformatics/btp449

Source DB:  PubMed          Journal:  Bioinformatics        ISSN: 1367-4803            Impact factor:   6.937


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