Quantitative NMR Studies of High Molecular Weight Proteins: Application to Domain Orientation and Ligand Binding in the 723 Residue Enzyme Malate Synthase G

This publication has 52 references indexed in Scilit:

• Crystal Structure of Escherichia coli Malate Synthase G Complexed with Magnesium and Glyoxylate at 2.0 Å Resolution: Mechanistic Implications^,,
  Biochemistry, 2000
• Ligand-Induced Domain Movement in Pyruvate Kinase: Structure of the Enzyme from Rabbit Muscle with Mg2+, K+, andl-Phospholactate at 2.7 Å Resolution
  Archives of Biochemistry and Biophysics, 1997
• Ligand binding on to maize (Zea mays) malate synthase: a structural study
  Biochemical Journal, 1994
• Molecular Characterization of Escherichia coli Malate Synthase G
  European Journal of Biochemistry, 1994
• Structure of Rabbit Muscle Pyruvate Kinase Complexed with Mn2+, K+, and Pyruvate
  Biochemistry, 1994
• Crystallographic refinement and atomic models of two different forms of citrate synthase at 2·7 and 1·7 Å resolution
  Journal of Molecular Biology, 1982
• Small-angle X-ray studies on malate synthase from Baker's yeast
  Biochemical and Biophysical Research Communications, 1977
• Molecular structure of malate synthase and structural changes upon ligand binding to the enzyme
  Biochemical and Biophysical Research Communications, 1974
• Asymmetric Methyl Groups: Preparation and Detection of Chiral Methyl Groups
  Nature, 1969
• Asymmetric Methyl Groups: Asymmetric Methyl Groups, and the Mechanism of Malate Synthase
  Nature, 1969