
doi: 10.1038/267585a0
pmid: 301613
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.
Models, Molecular, Time Factors, Fourier Analysis, Protein Conformation, Biophysics, Proteins, Biophysical Phenomena, Motion, Aprotinin, X-Ray Diffraction, Solvents, Thermodynamics
Models, Molecular, Time Factors, Fourier Analysis, Protein Conformation, Biophysics, Proteins, Biophysical Phenomena, Motion, Aprotinin, X-Ray Diffraction, Solvents, Thermodynamics
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