Formation of short-lived protein aggregates directly from the coil in two-state folding.

Abstract:

:Recent results on the 102 residue protein U1A show that protein aggregation is not always slow and irreversible but may take place transiently in refolding studies on a millisecond time scale. In this study we observe a similar aggregation behavior with the classical two-state protein CI2. Since both U1A and CI2 appear to fold directly from the coil at low protein concentrations, it is likely that the aggregates also form directly from the coil. This is in contrast to the behavior of larger multistate proteins where aggregation occurs in connection to "sticky" intermediates.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Silow M,Tan YJ,Fersht AR,Oliveberg M

doi

10.1021/bi9909997

subject

Has Abstract

pub_date

1999-10-05 00:00:00

pages

13006-12

issue

40

eissn

0006-2960

issn

1520-4995

pii

bi9909997

journal_volume

38

pub_type

杂志文章