Abstract
The five-helix bundle γ-repressor fragment is a fast-folding protein. A length of 80 amino acid residues puts it on the large end among all known microsecond folders, and its size poses a computational challenge for molecular dynamics (MD) studies. We simulated the folding of a novel γ-repressor fast-folding mutant (γ-HG) in explicit solvent using an all-atom description. By means of a recently developed tempering method, we observed reversible folding and unfolding of γ-repressor in a 10 μs trajectory. The folding kinetics was also investigated through a set of MD simulations run at different temperatures that together covered more than 125 μs. The protein was seen to fold into a native-like topology at intermediate temperature, and a slow-folding pathway was identified. The simulations suggest new experimental observables for better monitoring of the folding process, and a novel mutation is expected to accelerate γ-repressor folding.
Original language | English (US) |
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Pages (from-to) | 1117-1123 |
Number of pages | 7 |
Journal | Journal of Physical Chemistry Letters |
Volume | 3 |
Issue number | 9 |
DOIs | |
State | Published - May 3 2012 |
ASJC Scopus subject areas
- Materials Science(all)
- Physical and Theoretical Chemistry