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Title: Solvent viscosity effects on the rate of side-chain rotational isomerization in a protein molecule

Journal Article · · J. Phys. Chem.; (United States)
DOI:https://doi.org/10.1021/j100303a003· OSTI ID:5954332

The activated rotation of the tyrosine 35 ring in bovine pancreatic trypsin inhibitor has been simulated in model solvents that have extremely different viscosities but that are otherwise identical. Both simulations are at 300 K, but one solvent corresponds to liquid water and the other to a hypothetical glassy water. Although the ring is located in the surface region of the protein, the freezing of the solvents reduces the rate constant for rotation by only 50%. The time required to complete individual transitions is somewhat lengthened, apparently due to slowed relaxation both of ring-solvent interactions and of the conformation of the protein matrix that surrounds most of the ring. The slowing of these relaxations also leads to the reduction in the rate constant: the persistence of ring environments that favor rotation increases the likelihood that the ring will return to the transition-state region soon after passing through it, rather than being trapped in a stable state.

Research Organization:
Univ. of Houston, TX
OSTI ID:
5954332
Journal Information:
J. Phys. Chem.; (United States), Vol. 91:19
Country of Publication:
United States
Language:
English

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