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PMID: 301613 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Dynamics of folded proteins.

Nature ·Vol. 267 ·No. 5612 ·1977-06-16 ·Pages 585-90

McCammon JA, Gelin BR, Karplus M

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.

MeSH Terms
Aprotinin Biophysical Phenomena Biophysics Fourier Analysis Models, Molecular Motion Protein Conformation Proteins Solvents Thermodynamics Time Factors X-Ray Diffraction
Chemicals
Proteins Solvents Aprotinin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
McCammon J A
Gelin B R
Karplus M
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1977-06-16
Pages
585-90
Language
English
Region
England
NLM ID
0410462
Subset
IM
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