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- W3023776952 abstract "Two-state folding and down-hill folding are two kinds of protein folding dynamics for small single domain proteins. Here we apply molecular dynamics (MD) simulation to the two-state protein GB1 and down-hill folding protein gpW to reveal the relationship of their free energy landscape and folding/unfolding dynamics. Results from the steered MD simulations show that gpW is much less mechanical resistant than GB1, and the unfolding process of gpW has more variability than that of GB1 according to their force–extension curves. The potential of mean force (PMF) of GB1 and gpW obtained by the umbrella sampling simulations shows apparent difference: PMF of GB1 along the coordinate of extension exhibits a kink transition point where the slope of PMF drops suddenly, while PMF of gpW increases with extension smoothly, which are consistent with two-state folding dynamics of GB1 and downhill folding dynamics of gpW, respectively. Our results provide insight to understand the fundamental mechanism of different folding dynamics of two-state proteins and downhill folding proteins." @default.
- W3023776952 created "2020-05-13" @default.
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- W3023776952 date "2020-06-01" @default.
- W3023776952 modified "2023-09-22" @default.
- W3023776952 title "Different potential of mean force of two-state protein GB1 and downhill protein gpW revealed by molecular dynamics simulation*" @default.
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- W3023776952 doi "https://doi.org/10.1088/1674-1056/ab8daf" @default.
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