Dynamics of folded proteins
- 1 June 1977
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 267 (5612) , 585-590
- https://doi.org/10.1038/267585a0
Abstract
The dynamics of a folded globular protein (bovine pancreatic trypsin inhibitor) were 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.This publication has 38 references indexed in Scilit:
- Fluorotyrosine alkaline phosphatase: Internal mobility of individual tyrosines and the role of chemical shift anisotropy as a 19F nuclear spin relaxation mechanism in proteinsPublished by Elsevier ,2006
- Temperature dependent molecular motion of a tyrosine residue of ferrocytochrome CFEBS Letters, 1976
- Conformation of immunoglobulin M. 2. Nanosecond fluorescence depolarization analysis of segmental flexibility in anti-iε-1-dimethylamino-5-naphthalenesulfonyl-L-lysine anti-immunoglobulin from horse, pig, and sharkBiochemistry, 1976
- Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studiesBiochemistry, 1976
- Hydrogen Exchange Studies of Respiratory ProteinsPublished by Elsevier ,1974
- Room Temperature Phosphorescence and the Dynamic Aspects of Protein StructureProceedings of the National Academy of Sciences, 1974
- An Approach for the Determination of Equilibrium Constant of Structural MotilityEuropean Journal of Biochemistry, 1974
- Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scaleBiochemistry, 1973
- Conformationally Dependent Low-Frequency Motions of Proteins by Laser Raman SpectroscopyProceedings of the National Academy of Sciences, 1972
- Segmental flexibility in an antibody moleculeJournal of Molecular Biology, 1970