Dynamics of folded proteins
JA McCammon, BR Gelin, M Karplus - nature, 1977 - nature.com
JA McCammon, BR Gelin, M Karplus
nature, 1977•nature.comThe 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.
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.
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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