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Dynamics of folded proteins

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Abstract

The dynamics of a folded globular protein (bovine pancreatic trypsin inhibitor) have been studied by solving the equations of motion for the atoms with an empirical potential energy function. The results provide the magnitude, correlations and decay of fluctuations about the average structure. These suggest that the protein interior is fluid-like in that the local atom motions have a diffusional character.

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Authors and Affiliations

  1. Department of Chemistry, Harvard University, Cambridge, Massachusetts, 02138

    J. Andrew McCammon, Bruce R. Gelin & Martin Karplus

Authors
  1. J. Andrew McCammon
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  2. Bruce R. Gelin
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  3. Martin Karplus
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McCammon, J., Gelin, B. & Karplus, M. Dynamics of folded proteins. Nature 267, 585–590 (1977). https://doi.org/10.1038/267585a0

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