Two-state protein model with water interactions: Influence of temperature on the intrinsic viscosity of myoglobin
We describe a single-domain protein as a two-state system with water interactions. Around the unfolded apolar parts of the protein we incorporate the hydration effect by introducing hydrogen bonds between the water molecules in order to mimic the {open_quotes}icelike{close_quotes} shell structure. Intrinsic viscosity, proportional to the effective hydrodynamic volume, for sperm whale metmyoglobin is assigned from experimental data in the folded and in the denaturated state. By weighing statistically the two states against the degree of folding, we express the total intrinsic viscosity. The temperature dependence of the intrinsic viscosity, for different chemical potentials, is in good correspondence with experimental data [P. L. Privalov , J. Mol. Biol. >190, 487 (1986)]. Cold and warm unfolding, common to small globular proteins, is also a result of the model.
- Sponsoring Organization:
- (US)
- OSTI ID:
- 40203385
- Journal Information:
- Physical Review E, Vol. 63, Issue 6; Other Information: DOI: 10.1103/PhysRevE.63.061906; Othernumber: PLEEE8000063000006061906000001; 147106PRE; PBD: Jun 2001; ISSN 1063-651X
- Publisher:
- The American Physical Society
- Country of Publication:
- United States
- Language:
- English
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