Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/23177
Title: Cold shock domain of the human Y-box protein YB-1. Backbone dynamics and equilibrium between the native state and a partially unfolded state.
Authors: Kloks, CP
Tessari, M
Vuister, GW
Hilbers, CW
First Published: 10-Aug-2004
Citation: BIOCHEMISTRY, 2004, 43 (31), pp. 10237-10246
Abstract: The three-dimensional structure of the central cold shock domain (CSD) of the human Y-box protein (YB-1 CSD) is virtually identical to those available for the bacterial cold shock proteins (Csp's). We have further characterized YB-1 CSD by studying its dynamics by nuclear magnetic resonance. The observed structural similarity is reflected in the backbone dynamics, which for YB-1 CSD is very similar to that of the Escherichia coli protein CspA. The rotational correlation time of YB-1 CSD shows that it is a monomer. This indicates that the dimerization observed for the YB-1 protein is not caused by its CSD, but involves other parts of this protein. The YB-1 CSD is only marginally stable as are the mesophilic bacterial Csp's. In contrast to the rapid two-state folding of the bacterial Csp's, the formation of the native form of YB-1 CSD is slow and at least a three-state process. The NMR experiments revealed the presence of a second state of YB-1 CSD in equilibrium with the native form. The exchange rates from and to the folded state are in the order of 0.2 and 0.5 s(-1), respectively. Relaxation experiments indicated that the second state is a highly flexible, partly structured molecule.
DOI Link: 10.1021/bi049524s
ISSN: 0006-2960
Links: http://hdl.handle.net/2381/23177
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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