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Robustness of protein folding kinetics to surface hydrophobic substitutions

Published online by Cambridge University Press:  01 December 1999

H. GU ,
N. DOSHI ,
D.E. KIM ,
K.T. SIMONS ,
J.V. SANTIAGO ,
S. NAULI  and
DAVID BAKER
H. GU
Affiliation:
Department of Biochemistry, University of Washington, Seattle, Washington 98195
N. DOSHI
Affiliation:
Department of Biochemistry, University of Washington, Seattle, Washington 98195
D.E. KIM
Affiliation:
Department of Biochemistry, University of Washington, Seattle, Washington 98195
K.T. SIMONS
Affiliation:
Department of Biochemistry, University of Washington, Seattle, Washington 98195
J.V. SANTIAGO
Affiliation:
Department of Biochemistry, University of Washington, Seattle, Washington 98195
S. NAULI
Affiliation:
Department of Biochemistry, University of Washington, Seattle, Washington 98195
DAVID BAKER
Affiliation:
Department of Biochemistry, University of Washington, Seattle, Washington 98195
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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.

Keywords

binary patternphage displayprotein foldingprotein LSH3 domain
Type
Research Article
Information
Protein Science , Volume 8 , Issue 12 , December 1999 , pp. 2734 - 2741
Copyright
© 1999 The Protein Society

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