The contribution of the residues from the main hydrophobic core of ribonuclease A to its pressure-folding transition state.

ABSTRACT: The role of hydrophobic interactions established by the residues that belong to the main hydrophobic core of ribonuclease A in its pressure-folding transition state was investigated using the Phi-value method. The folding kinetics was studied using pressure-jump techniques both in the pressurization and depressurization directions. The ratio between the folding activation volume and the reaction volume (beta p-value), which is an index of the compactness or degree of solvation of the transition state, was calculated. All the positions analyzed presented fractional Phi f-values, and the lowest were those corresponding to the most critical positions for the ribonuclease A stability. The structure of the transition state of the hydrophobic core of ribonuclease A, from the point of view of for

SUBMITTER: Font J 

PROVIDER: S-EPMC2242501 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature