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Side-Chain Orientation and Hydrogen-Bonding Imprint Supra-τc Motion on the Protein Backbone of Ubiquitin

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Farès,  C.
Max Planck Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany, Fax: (+49) 551-201-2202;
Service Department Farès (NMR), Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Citation

Lakomek, N., Farès, C., Becker, S., Carlomango, T., Meiler, J., & Griesinger, C. (2005). Side-Chain Orientation and Hydrogen-Bonding Imprint Supra-τc Motion on the Protein Backbone of Ubiquitin. Angewandte Chemie International Edition: a journal of the Gesellschaft Deutscher Chemiker, 44(47), 7776-7778. doi:10.1002/anie.200502573.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-4B32-A
Abstract
Thumbnail image of graphical abstract Order parameters derived from residual dipolar couplings between NH groups reveal motion of protein backbones on a time scale slower than the correlation time τC. Less-mobile amides (blue and green) in ubiquitin, for example, are H-bonded and belong to residues with side chains pointing towards the hydrophobic core while more mobile ones (yellow, orange, and red) have solvent-exposed side chains and fewer H bonds.