Combining thermostable mutations increases the stability of lambda repressor.
Biochemistry
; 27(19): 7571-4, 1988 Sep 20.
Article
em En
| MEDLINE
| ID: mdl-3061460
ABSTRACT
We have combined three mutations previously shown to stabilize lambda repressor against thermal denaturation. Two of these mutations are in helix 3, where Gly-46 and Gly-48 have been replaced by alanines [Hecht, M. H., et al. (1986) Proteins Struct., Funct., Genet. 1, 43-46]. The other mutation, which replaces Tyr-88 with cysteine, allows the protein to form an intersubunit disulfide bond [Sauer, R. T., et al. (1986) Biochemistry 25, 5992-5998]. Calorimetric measurements show that the two alanine substitutions stabilize repressor by about 8 degrees C, that the disulfide bond stabilizes repressor by about 8 degrees C, and that the triple mutant is 16 degrees C more stable than wild-type repressor.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Repressoras
/
Fatores de Transcrição
/
Proteínas de Ligação a DNA
/
Temperatura Alta
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
1988
Tipo de documento:
Article