| dc.creator |
Mandala, Venkata S |
|
| dc.creator |
Hong, Mei |
|
| dc.date |
2021-09-20T18:22:09Z |
|
| dc.date |
2021-09-20T18:22:09Z |
|
| dc.date |
2020-10-19T14:25:42Z |
|
| dc.date.accessioned |
2023-03-01T18:04:58Z |
|
| dc.date.available |
2023-03-01T18:04:58Z |
|
| dc.identifier |
https://hdl.handle.net/1721.1/132388 |
|
| dc.identifier.uri |
http://localhost:8080/xmlui/handle/CUHPOERS/278677 |
|
| dc.description |
© 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. |
|
| dc.format |
application/pdf |
|
| dc.language |
en |
|
| dc.publisher |
Elsevier BV |
|
| dc.relation |
10.1016/J.SBI.2019.03.027 |
|
| dc.relation |
Current Opinion in Structural Biology |
|
| dc.rights |
Creative Commons Attribution-NonCommercial-NoDerivs License |
|
| dc.rights |
http://creativecommons.org/licenses/by-nc-nd/4.0/ |
|
| dc.source |
PMC |
|
| dc.title |
High-sensitivity protein solid-state NMR spectroscopy |
|
| dc.type |
Article |
|
| dc.type |
http://purl.org/eprint/type/JournalArticle |
|