| Abstract
| - On the basis of the measurement of NH residual dipolar couplings (RDCs) in 11 different alignmentmedia, an RDC-based order parameter is derived for each residue in the protein ubiquitin. Dipolar couplingsare motionally averaged in the picosecond to millisecond time range and, therefore, reflect motion slowerthan the inverse overall tumbling correlation time of the protein. It is found that there is considerable motionthat is slower than the correlation time and could not be detected with previous NMR methodology.Amplitudes and anisotropies of the motion can be derived from the model-free analysis. The method canbe applied provided that at least five sufficiently different alignment media can be found for the biomoleculeunder investigation.
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