TROSY-driven NMR backbone assignments of the 381-residue nucleotide-binding domain of the Thermus Thermophilus DnaK molecular chaperone

J Biomol NMR. 2004 Sep;30(1):113-4. doi: 10.1023/B:JNMR.0000042961.48233.f9.
No abstract available

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Cloning, Molecular
  • Escherichia coli / genetics
  • HSP70 Heat-Shock Proteins / chemistry*
  • HSP70 Heat-Shock Proteins / genetics
  • HSP70 Heat-Shock Proteins / metabolism
  • Hydrogen-Ion Concentration
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism
  • Molecular Sequence Data
  • Molecular Weight
  • Nuclear Magnetic Resonance, Biomolecular*
  • Nucleotides / metabolism*
  • Plasmids
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Temperature
  • Thermus thermophilus / chemistry*

Substances

  • HSP70 Heat-Shock Proteins
  • Molecular Chaperones
  • Nucleotides