Molecular Simulation of ab Initio Protein Folding for a Millisecond Folder NTL9(1-39)

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Abstract/Contents

Abstract: To date, the slowest-folding proteins folded ab initio by all-atom molecular dynamics simulations with fidelity to experimental kinetics have had folding times in the range of nanoseconds to microseconds. These include the designed mini-protein Trp-cage (∼4.1 μs), the villin headpiece domain (∼10 μs), a fast-folding variant of villin (<1 μs), and Fip35 WW domain (∼13 μs). In this communication, we report simulations of several folding trajectories, each from fully unfolded states, of the 39-residue protein NTL9(1-39), which experimentally has a folding time of ∼1.5 ms.

Type of resource	software, multimedia
Date created	October 8, 2009

Related Publication	Voelz, V. A., Bowman, G. R., Beauchamp, K. & Pande, V. S. Molecular Simulation of ab Initio Protein Folding for a Millisecond Folder NTL9(1−39). J. Am. Chem. Soc. 132, 1526–1528 (2010).
Related item	Title Pubmed Entry
Location	https://purl.stanford.edu/pt997zr0498

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Preferred Citation: Voelz, V. A., Bowman, G. R., Beauchamp, K. & Pande, V. S. (2009). Molecular Simulation of ab Initio Protein Folding for a Millisecond Folder NTL9(1-39). Stanford Digital Repository. Available at: http://purl.stanford.edu/pt997zr0498

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