Dynamics of folded proteins.

J A McCammon; B R Gelin; M Karplus

doi:10.1038/267585a0

PubMed · 301613

Dynamics of folded proteins.

J A McCammon·B R Gelin·M Karplus

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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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Aprotinin Biophysical Phenomena Biophysics Fourier Analysis Models, Molecular Motion Protein Conformation Proteins Solvents Thermodynamics Time Factors X-Ray Diffraction Journal Article Research Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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J A McCammon, B R Gelin, M Karplus. 1977-06-16. Dynamics of folded proteins.. https://doi.org/10.1038/267585a0

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Dynamics of folded proteins.

Abstract

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