High-sensitivity protein solid-state NMR spectroscopy
Name
nihms-1526024.pdf
Description
Accepted version
Size
581.27 KB
Format
Unknown
Checksum (MD5)
59ffb859482081e92c9a07420e60bb38
Author(s)
Mandala, Venkata Shiva
Hong, Mei
Date Issued
April 2019
Journal
Current Opinion in Structural Biology
Publisher
Elsevier BV
Version
Author's final manuscript
Abstract
© 2019 Elsevier Ltd The sensitivity of solid-state nuclear magnetic resonance (SSNMR) spectroscopy for structural biology is significantly increased by 1H detection under fast magic-angle spinning (MAS) and by dynamic nuclear polarization (DNP) from electron spins to nuclear spins. The former allows studies of the structure and dynamics of small quantities of proteins under physiological conditions, while the latter permits studies of large biomolecular complexes in lipid membranes and cells, protein intermediates, and protein conformational distributions. We highlight recent applications of these two emerging SSNMR technologies and point out areas for future development.
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.2019.03.027
