6533b7d8fe1ef96bd126a26b
RESEARCH PRODUCT
Inter- and intramolecular motions in proteins
Fritz G. Paraksubject
Quantitative Biology::BiomoleculesAbsorption spectroscopyScatteringProtein dynamicsCondensed Matter PhysicsAtomic and Molecular Physics and OpticsRoot mean squarechemistry.chemical_compoundAmplitudeNuclear magnetic resonanceMyoglobinchemistryChemical physicsIntramolecular forcePhysical and Theoretical ChemistryProtein crystallizationdescription
The use of 57 Fe Mossbauer radiation allows the study of protein crystal dynamics by a time-resolved analysis of X-ray scattering. In myoglobin crystals, the main source of the root mean squared amplitude of motions come from intramolecular protein dynamics. Segments of the size of an α-helix move collectively. Long-range correlated motions give only a minor contribution. Comparison with Mossbauer absorption spectroscopy shows that protein-specific dynamics is frozaen out below 200 K and the lattice dynamics in mainly responsible for the low-temperature behavior
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1992-06-05 | International Journal of Quantum Chemistry |