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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.
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Lakomek et al. (2005) studied this question.
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