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Side‐Chain Orientation and Hydrogen‐Bonding Imprint Supra‐ τ c Motion on the Protein Backbone of Ubiquitin
Author(s) -
Lakomek Nils A.,
Farès Christophe,
Becker Stefan,
Carlomagno Teresa,
Meiler Jens,
Griesinger Christian
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200502573
Subject(s) - side chain , hydrogen bond , ubiquitin , chemistry , dipole , solvent , residual , crystallography , residual dipolar coupling , computer science , stereochemistry , molecule , biochemistry , organic chemistry , algorithm , gene , polymer
Order parameters derived from residual dipolar couplings between NH groups reveal motion of protein backbones on a time scale slower than the correlation time τ C . 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.