Letter | Published:

A diffusion–collision–adhesion model for the kinetics of myoglobin refolding

Nature volume 286, pages 632634 (07 August 1980) | Download Citation

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Abstract

There are two distinct experimental and theoretical problems of protein folding: the thermodynamic issue of characterizing the folded state, and the kinetic question of the path between the unfolded and native states1. Here we consider the second question and present a diffusion–collision–adhesion model for the folding of the α-helical protein myoglobin. In particular, we consider the fast refolding species of the unfolded state and ignore the slow transition between unfolded states that has been attributed to proline isomerization2.

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Author information

Affiliations

  1. Laboratory of Molecular Biophysics, Department of Zoology, South Parks Road, Oxford OX1 3PS, UK

    • F. E. Cohen
    • , M. J. E. Sternberg
    •  & D. C. Phillips
  2. Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, California 94143

    • I. D. Kuntz
    •  & P. A. Kollman
  3. Present address: Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, California.

    • F. E. Cohen

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DOI

https://doi.org/10.1038/286632a0

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