Please use this identifier to cite or link to this item: https://doi.org/10.1021/bi9909997
Title: Formation of short-lived protein aggregates directly from the coil in two-state folding
Authors: Silow, M.
Tan, Y.-J. 
Fersht, A.R.
Oliveberg, M.
Issue Date: 5-Oct-1999
Citation: Silow, M., Tan, Y.-J., Fersht, A.R., Oliveberg, M. (1999-10-05). Formation of short-lived protein aggregates directly from the coil in two-state folding. Biochemistry 38 (40) : 13006-13012. ScholarBank@NUS Repository. https://doi.org/10.1021/bi9909997
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.
Source Title: Biochemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/111889
ISSN: 00062960
DOI: 10.1021/bi9909997
Appears in Collections:Staff Publications

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