Folding kinetics of WW domains with the united residue force field for bridging microscopic motions and experimental measurements.

Volume: 111, Issue: 51, Pages: 18243 - 18248
Published: Dec 23, 2014
Abstract
To demonstrate the utility of the coarse-grained united-residue (UNRES) force field to compare experimental and computed kinetic data for folding proteins, we have performed long-time millisecond-timescale canonical Langevin molecular dynamics simulations of the triple β-strand from the Formin binding protein 28 WW domain and six nonnatural variants, using UNRES. The results have been compared with available experimental data in both a...
Paper Details
Title
Folding kinetics of WW domains with the united residue force field for bridging microscopic motions and experimental measurements.
Published Date
Dec 23, 2014
Volume
111
Issue
51
Pages
18243 - 18248
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