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  • American Institute of Physics (AIP)  (2)
  • 1
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 112 (2000), S. 4394-4401 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The coil α-helix (and reverse) transition in peptides is modeled as a sequential diffusive kinetic process in which the fundamental event is the diffusion back and forth over a square barrier to propagate or dissolve a single hydrogen bond. The model is solved exactly numerically in one-dimension (the reaction coordinate), for helix and coil probabilities as a function of (1) time, (2) the number of hydrogen bonds, and (3) temperature. In addition, a modified first-passage time is calculated as the time scale of the coil to helix transition. The results of the diffusion model calculations are compared with recent experiments and we show how the model may give insight into protein folding kinetics. The mechanistic diffusion model complements the Master equation model applied previously to the coil–helix folding problem and provides insight into the choice of a useful reaction coordinate for the process. © 2000 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 116 (2002), S. 418-426 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Protein folding is modeled as one-dimensional diffusion in a potential with square wells representing folding species and square barriers representing transitions among the species. Within the context of the model, one or more intermediate species can either speed up or slow down folding, depending on their energy and on the potential barrier(s) to the final folded state. Intermediate species in deep potential wells may reduce the probability in the final state, as well as slowing the overall folding process. The potential barrier model is consistent with protein folding taking place by diffusion, collision and coalescence of marginally stable subunits of the protein in a sequential but, in principle, arbitrary order, as in the diffusion-collision model. Using parameters taken from the structures of three-helix bundle proteins the potential barrier model gives folding rates consistent with recent experiments on these proteins. © 2002 American Institute of Physics.
    Type of Medium: Electronic Resource
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