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Article

Kinetic network models of tryptophan mutations in β-hairpins reveal the importance of non-native interactions.

Journal of chemical theory and computation - 9 Jun 2015

Razavi Asghar M, Voelz Vincent A

Abstract excerpt

We present an analysis of the most extensive explicit-solvent simulations of β-hairpins to date (9.4 ms in aggregate), with the aim of probing the effects of tryptophan mutations on folding. From molecular simulations of GB1 hairpin, trpzip4, trpzip5, and trpzip6 performed on Folding@home, Markov State Models (MSMs) were constructed using a unified set of metastable states, enabling objective comparison of...

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Kinetics
Markov Chains
Molecular Dynamics Simulation
Mutation
Protein Folding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Structure, Secondary

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PMID: 26575573
DOI: 10.1021/acs.jctc.5b00088

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