Robustness of protein folding kinetics to surface hydrophobic substitutions

TitleRobustness of protein folding kinetics to surface hydrophobic substitutions
Publication TypeJournal Article
Year of Publication1999
AuthorsGu, H., Doshi N., Kim D. E., Simons K. T., Santiago J. V., Nauli S., & Baker D.
JournalProtein science
Date Published1999 Dec
KeywordsAmino Acid Substitution, Bacterial Proteins, Combinatorial Chemistry Techniques, DNA-Binding Proteins, Kinetics, Mutagenesis, Site-Directed, Peptostreptococcus, Primary Publication, Protein Folding, Protein Structure, Secondary, src Homology Domains

We use both combinatorial and site-directed mutagenesis to explore the consequences of surface hydrophobic substitutions for the folding of two small single domain proteins, the src SH3 domain, and the IgG binding domain of Peptostreptococcal protein L. We find that in almost every case, destabilizing surface hydrophobic substitutions have much larger effects on the rate of unfolding than on the rate of folding, suggesting that nonnative hydrophobic interactions do not significantly interfere with the rate of core assembly.

Alternate JournalProtein Sci.
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