It is a major asset of NMR spectroscopy in solution that it enables complementation of information on the architecture of biological macromolecules with data on conformational equilibria, and on intra- and inter-molecular rate processes. This lecture will focus on intra-molecular polymorphisms and rate processes. In addition to high-frequency events, in the range of the time scale of the rotational Brownian motions of the molecules considered, “ring flips” of phenylalanine and tyrosine in globular proteins fall into a second NMR-accessible range of rate processes, from microseconds to seconds. NMR observation and computational modeling of ring flips will be discussed and related to other observations on dynamic processes in biological macromolecules.
References
Wüthrich, K. and Wagner, G. (1975) FEBS Lett. 50, 265–268. NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor.
Shaw, D.E., Maragakis, P., Lindoff-Larsen, K., Pianna, S., Dror, R.O., Eastwood M.P., Bank, J.A., Jumper, J.M., Salmon, J.K., Shan, Y and Wriggers, W. (2010) Science 330, 341–346. Atomic-level characterization of the structural dynamics of proteins.
Martin, B.T., Serrano, P., Geralt, M. and Wüthrich K. (2016) Structure 24, 158–164. Nuclear magnetic resonance structure of a novel globular domain in RBM10 containing OCRE, the octamer repeat sequence motif.
