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Is an intermediate state populated on the folding pathway of ubiquitin?

Heather M Went, Claudia G Benitez-Cardoza, and Sophie E Jackson

FEBS Lett 567(2-3):6 (2004) PMID 15178347

In the last couple of years, there has been increasing debate as to the presence and role of intermediate states on the folding pathways of several small proteins, including the 76-residue protein ubiquitin. Here, we present detailed kinetic studies to establish whether an intermediate state is ever populated during the folding of this protein. We show that the differences observed in previous studies are attributable to the transient aggregation of the protein during folding. Using a highly soluble construct of ubiquitin, which does not aggregate during folding, we establish the conditions in which an intermediate state is sufficiently stable to be observed by kinetic measurements.

Copyright © 2004 Elsevier Ltd. All rights reserved.

DOI: 10.1016/j.febslet.2004.04.089
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