Dynamics of folded proteins

Dynamics of folded proteins

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...

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Veröffentlicht in:Nature (London) 1977-06, Vol.267 (5612), p.585-590
Hauptverfasser: McCammon, J. Andrew, Gelin, Bruce R, Karplus, Martin
Format: Artikel
Sprache:eng
Schlagworte:
Aprotinin
Biophysical Phenomena
Biophysics
Fourier Analysis
Models, Molecular
Motion
Protein Conformation
Proteins
Solvents
Thermodynamics
Time Factors
X-Ray Diffraction
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Zusammenfassung: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/267585a0