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

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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 notes

  1. F. E. Cohen

    Present address: Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, California

Authors and 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

Authors
  1. F. E. Cohen
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  2. M. J. E. Sternberg
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  3. D. C. Phillips
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  4. I. D. Kuntz
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  5. P. A. Kollman
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Cohen, F., Sternberg, M., Phillips, D. et al. A diffusion–collision–adhesion model for the kinetics of myoglobin refolding. Nature 286, 632–634 (1980). https://doi.org/10.1038/286632a0

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

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