AI Article Synopsis
- Proteins rely on their motions to function properly, and aliphatic side chains are crucial for interactions with other molecules.
- A new NMR method allows researchers to measure the motions of methyl-bearing side chains in proteins at a very fine time scale, revealing significant motion types in the side chains of isoleucine within the protein ubiquitin.
- The findings, combined with molecular dynamics simulations, clarify how slow motions contribute to transitions between different states, enhancing our understanding of protein side-chain dynamics and their functions.
Article Abstract
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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/jacs.8b09107 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!