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Free keywords:
Kinetics, Models, Theoretical, Peptides, Protein Conformation, Protein Structure, Secondary
Abstract:
The time, temperature, and sequence dependences of helix formation kinetics of fully atomistic peptide models in explicit solvent are described quantitatively by a diffusive search within the coil state with barrierless transitions into the helical state. Conformational diffusion leads to nonexponential kinetics and jump-width dependences in temperature jump experiments.
