NMR assignments of the sylvatic dengue 1 virus envelope protein domain III

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.

Saved in:
Bibliographic Details
Published in:Biomolecular NMR assignments 2008-12, Vol.2 (2), p.155-157
Main Authors: Volk, David E., Anderson, Kurtis M., Gandham, Sai H. A., May, Fiona J., Li, Li, Beasley, David W. C., Barrett, Alan D. T., Gorenstein, David G.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biochemistry
Biological and Medical Physics
Biophysics
Carbon Isotopes - chemistry
Dengue fever
Dengue Virus - metabolism
Magnetic Resonance Spectroscopy - methods
Molecular biology
Molecular Sequence Data
Molecular Weight
Mutation
Nitrogen Isotopes - chemistry
NMR
Nuclear magnetic resonance
Physics
Physics and Astronomy
Polymer Sciences
Protein Structure, Tertiary
Proteins
Protons
Viral Envelope Proteins - chemistry
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-008-9109-5