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. 1984 Nov;81(22):7088–7092. doi: 10.1073/pnas.81.22.7088

A consistent picture of protein dynamics.

F Parak, E W Knapp
PMCID: PMC392082  PMID: 6594683

Abstract

Information about the protein dynamics of myoglobin obtained by x-ray and Mössbauer investigations is analyzed and compared with computer simulations. Computer simulations give correct amplitudes of mean-square displacements but fail in the description of the time dependence of motions. Our model describes protein dynamics at physiological temperatures as an overdamped diffusion-like motion in a restricted space. The fluctuations occur around the average conformation determined by x-ray structure analysis. The gain in entropy drives the molecule into the transition state and, in this way, accounts for its flexibility.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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