Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 140, Issue 41, Pages 13456-13465Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.8b09107
Keywords
-
Categories
Funding
- European Research Council (ERC) under the European Community's Seventh Framework Programme (FP7/2007-2013), ERC [279519]
- Equipex [ANR-10-EQPX-09]
- National Science Foundation [NSF MCB 1715505]
- TGIR-RMN-THC FR 3050 CNRS
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available