Probing residue-specific interactions in the stabilization of proteins using high-resolution NMR: a study of disulfide bond compensation.

ABSTRACT: It is well established that the oxidation state of cysteine residues in proteins is critical to overall physical stability. Disulfide bonds most often impart thermodynamic stability, but in some cases, diminish it. Predicting the circumstances that lead to each outcome is difficult because mechanistic information is lacking. Because the techniques typically used to study protein stability do not provide sufficient detail, high-resolution NMR was used in combination with low-resolution analysis to obtain mechanistic information regarding disulfide bond formation in a model protein. T(m) (CD) and T(onset) (SLS) for the reduced and oxidized wild type and C104S and C49S mutants were measured. The mutant proteins have altered T(m)s and T(onset)s compared to the reduced wild type, indicating tha

SUBMITTER: Skinner AL 

PROVIDER: S-EPMC3683975 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature