Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy
Name
nihms-1524584.pdf
Description
Accepted version
Size
826.15 KB
Format
Adobe PDF
Checksum (MD5)
db776b59c86ee90940404e64bab5e84f
Author(s)
Elkins, Matthew Ryan
Hong, Mei
Date Issued
August 2019
Journal
Current Opinion in Structural Biology
Publisher
Elsevier BV
Citation
Elkins, Matthew R. and Mei Hong. “Elucidating ligand-bound structures of membrane proteins using solid-state NMR spectroscopy.” Current Opinion in Structural Biology, 57 (August 2019): 103–109 © 2019 The Author(s)
Version
Author's final manuscript
Abstract
Magic-angle-spinning (MAS) solid-state NMR spectroscopy is a versatile technique to elucidate functionally important protein–ligand interactions in lipid membranes. Here, we review recent solid-state NMR studies of membrane protein interactions with cholesterol, lipids, transported substrates, and peptide ligands. These studies are conducted in synthetic or native lipid bilayers to provide an accurate environment for ligand binding. The solid-state NMR approaches include multinuclear detection to gain comprehensive structural information, distance measurements to locate ligand-binding sites, and dynamic nuclear polarization and 1 H detection to enhance spectral sensitivity. These studies provide novel insights into the mechanisms of virus budding, virus entry into cells, transmembrane signaling, substrate transport, antibacterial action, and many other biological processes.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivs License
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/J.SBI.2019.02.002
