Premium
Robustness of protein folding kinetics to surface hydrophobic substitutions
Author(s) -
Gu H.,
Doshi N.,
Kim D.E.,
Simons K.T.,
Santiago J.V.,
Nauli S.,
Baker David
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.12.2734
Subject(s) - kinetics , protein folding , robustness (evolution) , chemistry , biophysics , surface protein , biological system , protein structure , lattice protein , chemical physics , computational biology , biology , physics , biochemistry , classical mechanics , gene , virology
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.