Journal article
High-sensitivity protein solid-state NMR spectroscopy
Current opinion in structural biology, Vol.58, pp.183-190
10/01/2019
DOI: 10.1016/j.sbi.2019.03.027
PMCID: PMC6778492
PMID: 31031067
Abstract
The sensitivity of solid-state nuclear magnetic resonance (SSNMR) spectroscopy for structural biology is significantly increased by H-1 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.
Details
- Title: Subtitle
- High-sensitivity protein solid-state NMR spectroscopy
- Creators
- Venkata S. Mandala - Massachusetts Institute of TechnologyMei Hong - Massachusetts Institute of Technology
- Resource Type
- Journal article
- Publication Details
- Current opinion in structural biology, Vol.58, pp.183-190
- DOI
- 10.1016/j.sbi.2019.03.027
- PMID
- 31031067
- PMCID
- PMC6778492
- NLM abbreviation
- Curr Opin Struct Biol
- ISSN
- 0959-440X
- eISSN
- 1879-033X
- Publisher
- Current Biology Ltd
- Number of pages
- 8
- Grant note
- GM066976; GM088204 / N.I.H.; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA R01GM088204; R01GM066976 / NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of General Medical Sciences (NIGMS)
- Language
- English
- Date published
- 10/01/2019
- Academic Unit
- Biochemistry and Molecular Biology
- Record Identifier
- 9985113010802771
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