ausblenden:
Schlagwörter:
molecular dynamics; natural products; NMr spectrocopy; protein structures
Zusammenfassung:
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.
