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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,  Christophe
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Lakomek, N. A., Farès, C., Becker, S., Carlomagno, 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, 44(47), 7776-7778. doi:10.1002/anie.200502573.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-4B32-A
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.