Dynamics of folded proteins

Nature. 1977 Jun 16;267(5612):585-90. doi: 10.1038/267585a0.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aprotinin*
  • Biophysical Phenomena
  • Biophysics
  • Fourier Analysis
  • Models, Molecular
  • Motion
  • Protein Conformation
  • Proteins*
  • Solvents
  • Thermodynamics
  • Time Factors
  • X-Ray Diffraction

Substances

  • Proteins
  • Solvents
  • Aprotinin