Publication details
Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations
| Authors | |
|---|---|
| Year of publication | 2018 |
| Type | Article in Periodical |
| Magazine / Source | Journal of the American Chemical Society |
| MU Faculty or unit | |
| Citation | |
| web | https://pubs.acs.org/doi/10.1021/jacs.8b09107 |
| Doi | http://dx.doi.org/10.1021/jacs.8b09107 |
| Keywords | NUCLEAR MAGNETIC-RELAXATION; ORDER-PARAMETER ANALYSIS; C-13 NMR-SPECTROSCOPY; DEUTERIUM SPIN PROBES; METHYL-GROUP DYNAMICS; MODEL-FREE APPROACH; AMBER FORCE-FIELDS; SOLID-STATE NMR; CONFORMATIONAL ENTROPY; BACKBONE PARAMETERS |
| Description | Motions of proteins are essential for the performance of their functions. Aliphatic protein side chains and their motions play critical roles in protein interactions: for recognition and binding of partner molecules at the surface or serving as an entropy reservoir within the hydrophobic core. Here, we present a new NMR method based on high-resolution relaxometry and high-field relaxation to determine quantitatively both motional amplitudes and time scales of methyl-bearing side chains in the picosecond-to-nanosecond range. We detect a wide variety of motions in isoleucine side chains in the protein ubiquitin. We unambiguously identify slow motions in the low nanosecond range, which, in conjunction with molecular dynamics computer simulations, could be assigned to transitions between rotamers. Our approach provides unmatched detailed insight into the motions of aliphatic side chains in proteins and provides a better understanding of the nature and functional role of protein side-chain motions. |