Role of Adsorbed Water in the Dynamics of Metmyoglobin
- 31 August 1981
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 47 (9) , 685-688
- https://doi.org/10.1103/physrevlett.47.685
Abstract
By microwave measurements we have determined the dielectric relaxation rate for adsorbed water in metmyoglobin crystals in the temperature range from 100 to 300 K. The temperature dependence of the dielectric relaxation rate of the adsorbed water is nearly identical to the temperature dependence of the conformational fluctuation rate of the protein as measured by the Mössbauer effect. This surprising correlation may be understood in terms of the mechanical and electrical interactions between the adsorbed water and the protein.Keywords
This publication has 8 references indexed in Scilit:
- Fluctuations between conformational substates in deoxygenated myoglobinHyperfine Interactions, 1981
- Dynamics of metmyoglobin crystals investigated by nuclear gamma resonance absorptionJournal of Molecular Biology, 1981
- Evidence for Conformational and Diffusional Mean Square Displacements in Frozen Aqueous Solution of OxymyoglobinPhysical Review Letters, 1980
- Electrostatic stabilization in myoglobin. The pH dependence of summed electrostatic contributionsBiochemistry, 1979
- Temperature-dependent X-ray diffraction as a probe of protein structural dynamicsNature, 1979
- Further observations on the electrical properties of hemoglobin-bound waterThe Journal of Physical Chemistry, 1969
- The crystal structure of myoglobin III. Sperm-whale myoglobinProceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences, 1957
- Dielectric Properties of Ice and Solid D2OThe Journal of Chemical Physics, 1952