2H and 13C NMR studies on the temperature-dependent water and protein dynamics in hydrated elastin, myoglobin and collagen
| dc.creator | Lusceac, S. A. | |
| dc.creator | Herbers, C. R. | |
| dc.creator | Vogel, M. | |
| dc.date | 2009-04-28 | |
| dc.date.accessioned | 2026-07-07T13:09:27Z | |
| dc.date.available | 2026-07-07T13:09:27Z | |
| dc.description | 2H NMR spin-lattice relaxation and line-shape analyses are performed to study the temperature-dependent dynamics of water in the hydration shells of myoglobin, elastin, and collagen. | |
| dc.identifier | https://arxiv.org/abs/0904.4424 | |
| dc.identifier | http://arxiv.org/abs/0904.4424 | |
| dc.identifier.uri | http://salesiana.dossiersoluciones.com/handle/123456789/228739 | |
| dc.subject | Soft Condensed Matter | |
| dc.title | 2H and 13C NMR studies on the temperature-dependent water and protein dynamics in hydrated elastin, myoglobin and collagen | |
| dc.type | text |