Folding kinetics of phage T4 thioredoxin.
Biochemistry
; 29(12): 3071-7, 1990 Mar 27.
Article
en En
| MEDLINE
| ID: mdl-2186806
ABSTRACT
The folding mechanism for bacteriophage T4 thioredoxin is best described by a four-state box mechanism, N----Uc----Ut----It----N, where N indicates native, Uc the unfolded form with the cis proline isomer, Ut unfolded with the trans proline isomer, and It a compact form with a trans proline isomer. Both manual mixing fluorescence and size-exclusion chromatography indicate that there is a cis-trans proline isomerization that is important to the folding pathway. Furthermore, the data suggest that the cis-trans isomerization can also occur in a compact nativelike state which is referred to as It. The slow phase seen in fluorescence seems to be monitoring the cis-trans isomerization in the compact form, not the isomerization which occurs in the denatured state.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Fagos T
/
Tiorredoxinas
/
Proteínas Bacterianas
Idioma:
En
Revista:
Biochemistry
Año:
1990
Tipo del documento:
Article