The Origin of Nonmonotonic Complex Behavior and the Effects of Nonnative Interactions on the Diffusive Properties of Protein Folding
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Data
2010-07-21
Autores
Oliveira, Ronaldo J. [UNESP]
Whitford, Paul C.
Chahine, Jorge [UNESP]
Wang, Jin
Onuchic, Jose N.
Leite, Vitor Barbanti Pereira [UNESP]
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Cell Press
Resumo
We present a method for calculating the configurational-dependent diffusion coefficient of a globular protein as a function of the global folding process. Using a coarse-grained structure-based model, we determined the diffusion coefficient, in reaction coordinate space, as a function of the fraction of native contacts formed Q for the cold shock protein (TmCSP). We find nonmonotonic behavior for the diffusion coefficient, with high values for the folded and unfolded ensembles and a lower range of values in the transition state ensemble. We also characterized the folding landscape associated with an energetically frustrated variant of the model. We find that a low-level of frustration can actually stabilize the native ensemble and increase the associated diffusion coefficient. These findings can be understood from a mechanistic standpoint, in that the transition state ensemble has a more homogeneous structural content when frustration is present. Additionally, these findings are consistent with earlier calculations based on lattice models of protein folding and more recent single-molecule fluorescence measurements.
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Biophysical Journal. Cambridge: Cell Press, v. 99, n. 2, p. 600-608, 2010.