Nuclear magnetic resonance studies of the structure and binding sites of enzymes. II. Spectral assignments and inhibitor binding in hen egg-white lysozyme.

Lignende værker

• Observation of individual carboxyl groups in hen egg-white lysozyme by use of high field 13C-nuclear magnetic resonance.
  af: Shindo, H, et al.
  Udgivet: (1976)
• The simultaneous binding of lanthanide and N-acetylglucosamine inhibitors to hen egg-white lysozyme in solution by 1H and 13C nuclear magnetic resonance.
  af: Perkins, S J, et al.
  Udgivet: (1981)
• THE HEN EGG-WHITE LYSOZYME MOLECULE
  af: Phillips, David C.
  Udgivet: (1967)
• The binding of monosaccharide inhibitors to hen egg-white lysozyme by proton magnetic resonance at 270 MHz and analysis by ring-current calculations.
  af: Perkins, S J, et al.
  Udgivet: (1981)
• Pressure-assisted cold denaturation of hen egg white lysozyme: the influence of co-solvents probed by hydrogen exchange nuclear magnetic resonance
  af: K. Vogtt, et al.
  Udgivet: (2005-08-01)