Robustness of protein folding kinetics to surface hydrophobic substitutions.
Protein Sci
; 8(12): 2734-41, 1999 Dec.
Article
em En
| MEDLINE
| ID: mdl-10631990
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Dobramento de Proteína
/
Proteínas de Ligação a DNA
Idioma:
En
Revista:
Protein Sci
Assunto da revista:
BIOQUIMICA
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
Estados Unidos