Journal
PROTEIN SCIENCE
Volume 9, Issue 12, Pages 2394-2404Publisher
WILEY
DOI: 10.1110/ps.9.12.2394
Keywords
barnase; denatured states; disulfide bonds; molecular dynamics; NMR
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Funding
- NIGMS NIH HHS [GM 50789] Funding Source: Medline
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The effects of engineered disulfide bonds on protein stability are poorly understood because they can influence the structure, dynamics, and energetics of both the native and denatured states. To explore the effects of two engineered disulfide bonds on the stability of barnase, we have conducted a combined molecular dynamics and NMR study of the denatured state of the two mutants. As expected, the disulfide bonds constrain the denatured state. However, specific extended beta -sheet structure can also be detected in one of the mutant proteins. This mutant is also more stable than would be predicted. Our study suggests a possible cause of the very high stability conferred by this disulfide bond: the wild-type denatured ensemble is stabilized by a nonnative hydrophobic cluster, which is constrained from occurring in the mutant due to the formation of secondary structure.
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