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Is an intermediate state populated on the folding pathway of ubiquitin?
Author(s) -
Went Heather M.,
Benitez-Cardoza Claudia G.,
Jackson Sophie E.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.04.089
Subject(s) - ubiquitin , protein folding , phi value analysis , chemistry , folding (dsp implementation) , biophysics , folding funnel , intermediate state , lattice protein , residue (chemistry) , downhill folding , crystallography , biochemistry , biology , physics , atomic physics , electrical engineering , gene , engineering
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.