Strange kinetic phase in the extremely early folding process of beta-lactoglobulin.
FEBS Lett
; 581(23): 4463-7, 2007 Sep 18.
Article
in En
| MEDLINE
| ID: mdl-17761168
ABSTRACT
A continuous-wave probed laser-induced temperature jump system was constructed and applied to monitor the changes in tryptophan fluorescence of the beta-lactoglobulin during its folding; the kinetic phases were traced from 300 ns to 10 ms after a temperature jump. Notably, an early phase with typical squeezed-exponential characteristics, [exp[-(kt)(beta)], beta>1.0], was observed around several tens of microseconds after the temperature jump, which is actually the earliest phase ever observed for beta-lactoglobulin. This process can be explained by conformational shift occurring within the unfolded ensemble (U-->U'), which is followed by the non-native intermediate (I) formation of this protein.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Tryptophan
/
Protein Folding
/
Lactoglobulins
Language:
En
Journal:
FEBS Lett
Year:
2007
Document type:
Article
Affiliation country:
Japan