Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques.

Lignende værker

• Secondary structure of the phosphocarrier protein IIIGlc, a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy.
  af: Pelton, J G, et al.
  Udgivet: (1991)
• Three-dimensional structure of the Escherichia coli phosphocarrier protein IIIglc.
  af: Worthylake, D, et al.
  Udgivet: (1991)
• Site-directed mutagenesis of the phosphocarrier protein. IIIGlc, a major signal-transducing protein in Escherichia coli.
  af: Presper, K A, et al.
  Udgivet: (1989)
• Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN′ by NMR
  af: Day, Regina M., et al.
  Udgivet: (2003)
• The tautomeric state of histidines in myoglobin.
  af: Bhattacharya, S, et al.
  Udgivet: (1997)