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

Biomol NMR Assign. 2008 Dec;2(2):155-7. doi: 10.1007/s12104-008-9109-5. Epub 2008 Aug 12.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 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*

Substances

  • Carbon Isotopes
  • Nitrogen Isotopes
  • Protons
  • Viral Envelope Proteins