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
Biochemistryjournal_title
Biochemistryauthors
Silow M,Tan YJ,Fersht AR,Oliveberg Mdoi
10.1021/bi9909997subject
Has Abstractpub_date
1999-10-05 00:00:00pages
13006-12issue
40eissn
0006-2960issn
1520-4995pii
bi9909997journal_volume
38pub_type
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