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An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility

Durney, Michael A., Wechselberger, Rainer W., Kalodimos, Charalampos G., Kaptein, Robert, Vorgias, Constantinos E. and Boelens, Rolf (2004) An alternate conformation of the hyperthermostable HU protein from Thermotoga maritima has unexpectedly high flexibility FEBS Letters, 563, (1-3), pp. 49-54. (doi:10.1016/S0014-5793(04)00247-9).

Record type: Article


The homodimeric HU protein from the hyperthermophile Thermotoga maritima (HUTmar) is a model system which can yield insights into the molecular determinants of thermostability in proteins. Unusually for a thermostable protein, HUTmar exists in a structurally heterogeneous state as evidenced by the assignment of two distinct and approximately equally populated forms in solution. Relaxation measurements combined with chemical shift, hydrogen exchange, and nuclear Overhauser enhancement data confirm the main structural features of both forms. In addition, these data support a two-state model for HUTmar in which the major form closely resembles the X-ray structure while the very flexible minor form is less structured. HUTmar may therefore be a new example of the small class of hyperthermostable proteins with unexpected flexibility.

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Published date: 9 April 2004
Keywords: conformational flexibility, protein dynamics, thermostability, nuclear magnetic resonance spin relaxationdna-binding protein, histone-like protein, bacillus-stearothermophilus, spectroscopy, c-13, ihf, purification, resonance


Local EPrints ID: 20187
ISSN: 0014-5793
PURE UUID: 00b6c815-8a4e-404a-a64e-6520724c3720

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Date deposited: 22 Feb 2006
Last modified: 17 Jul 2017 16:29

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Author: Michael A. Durney
Author: Rainer W. Wechselberger
Author: Charalampos G. Kalodimos
Author: Robert Kaptein
Author: Constantinos E. Vorgias
Author: Rolf Boelens

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