| Abstract |
Nearly complete backbone and side chain resonance assignments have been obtained for the third domain, residues M289-K400, of the envelope protein from the sylvatic strain (P72-1244) of the dengue 1 virus, containing mutations N336S and E370K, using double- and triple-resonance spectroscopy. |
| Authors | David E Volk, Kurtis M Anderson, Sai H A Gandham, Fiona J May, Li Li, David W C Beasley, Alan D T Barrett, David G Gorenstein |
| Journal | Biomolecular NMR assignments
(Biomol NMR Assign)
Vol. 2
Issue 2
Pg. 155-7
(Dec 2008)
ISSN: 1874-270X [Electronic] Netherlands |
| PMID | 19636893
(Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
|
| Chemical References |
- Carbon Isotopes
- Nitrogen Isotopes
- Protons
- Viral Envelope Proteins
|
| Topics |
- Amino Acid Sequence
- Carbon Isotopes
(chemistry)
- Dengue Virus
(metabolism)
- Magnetic Resonance Spectroscopy
(methods)
- Molecular Sequence Data
- Molecular Weight
- Nitrogen Isotopes
(chemistry)
- Protein Structure, Tertiary
- Protons
- Viral Envelope Proteins
(chemistry)
|
