An essential intermediate in the folding of dihydrofolate reductase.
Proc Natl Acad Sci U S A
; 97(11): 5866-70, 2000 May 23.
Article
en En
| MEDLINE
| ID: mdl-10811909
The folding of Escherichia coli dihydrofolate reductase was examined at pH 7.8 and 15 degrees C by using stopped-flow fluorescence and absorbance spectroscopies. The formation of a highly fluorescent intermediate occurs with relaxation times ranging between 142 and 343 msec, whereas stopped-flow absorbance spectroscopy using methotrexate binding assays shows a distinct lag phase during these time frames for the native state. The lag in absorbance kinetics and the lack of fast-track folding events indicate that the formation of this ensemble of intermediates is an obligatory step in the folding reaction.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Tetrahidrofolato Deshidrogenasa
/
Proteínas Bacterianas
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Año:
2000
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Estados Unidos