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Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings

Meier, S. and Grzesiek, S. and Blackledge, M.. (2007) Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings. Journal of the American Chemical Society, Vol. 129, H. 31. pp. 9799-9807.

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Official URL: http://edoc.unibas.ch/dok/A5258766

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Abstract

Characterization of the unfolded state is a fundamental prerequisite for understanding protein stability and folding. We have investigated local conformational sampling in urea-denatured ubiquitin at pH 2.5 by measuring an extensive set of residual dipolar couplings (RDCs) under conditions of partial molecular alignment. Seven experimental RDCs per peptide unit, including complementary fixed-geometry and interproton (1H(N)-1H(N) and 1H(N)-1H(alpha)) couplings, were used to investigate the structural properties of the peptide chain. Amino-acid-specific potentials that simultaneously reproduce all RDCs in the molecule are found to sample more extended conformations than the standard statistical coil description. Analysis of 3J(HNHalpha) scalar couplings measured under the same conditions suggests that neither polyproline II nor extended beta-regions dominate this additional sampling of extended conformations. Using this approach we propose a model of the conformational landscape throughout the peptide chain of urea-denatured ubiquitin, providing an essential description for understanding the unfolded state.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Grzesiek)
UniBasel Contributors:Grzesiek, Stephan
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
ISSN:0002-7863
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:21

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