Work

Robustness of protein folding kinetics to surface hydrophobic substitutions

Year: 1999

Type: article

Abstract: 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.

Source: Protein Science

DOI: 10.1110/ps.8.12.2734

Authors: H. Gu, N. Doshi, D.E. Kim, K.T. Simons, J.V. Santiago, S. Nauli, David Baker

Institution: University of Washington

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Science Foundation, David and Lucile Packard Foundation, National Institutes of Health

OpenAlex ID: W2139462697

FWCI: 1.034

Cites: 22

Cited by: 23

Related to: 10