High-sensitivity protein solid-state NMR spectroscopy.
Curr Opin Struct Biol
; 58: 183-190, 2019 10.
Article
in En
| MEDLINE
| ID: mdl-31031067
ABSTRACT
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Proteins
/
Nuclear Magnetic Resonance, Biomolecular
Type of study:
Diagnostic_studies
Language:
En
Journal:
Curr Opin Struct Biol
Journal subject:
BIOLOGIA MOLECULAR
Year:
2019
Document type:
Article
Affiliation country:
United States