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High-sensitivity protein solid-state NMR spectroscopy

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sword-2020-10-19T14:25:42.original.xml (130 B)
Original SWORD entry document
Author(s)
Mandala, Venkata S
•
Hong, Mei
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.
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Creative Commons Attribution-NonCommercial-NoDerivs License
http://creativecommons.org/licenses/by-nc-nd/4.0/
Persistent DSpace Link
https://hdl.handle.net/1721.1/132388
DOI of Published Version
10.1016/J.SBI.2019.03.027
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