[9] Calorimetric methods for interpreting protein—Ligand interactions

This publication has 21 references indexed in Scilit:

• Thermodynamic effects of active-site ligands on the reversible, partial unfolding of dodecameric glutamine synthetase from Escherichia coli: calorimetric studies
  Biochemistry, 1992
• Crystal structure and ligand binding studies of a screened peptide complexed with streptavidin
  Biochemistry, 1992
• Heat capacity changes for protein-peptide interactions in the ribonuclease S system
  Biochemistry, 1992
• Calorimetric studies of the binding of ferric ions to ovotransferrin and interactions between binding sites
  Biochemistry, 1991
• Characterization of recombinant human renin: Kinetics,pH-stability, and peptidomimetic inhibitor binding
  Protein Journal, 1991
• Sensitive titration microcalorimetric study of the binding of Salmonella O‐antigenic oligosaccharides by a monoclonal antibody
  European Journal of Biochemistry, 1991
• Differential scanning calorimetry of a conformational transition in heavy meromyosin
  Archives of Biochemistry and Biophysics, 1990
• NADPH binding induced proton ionization as a cause of nonlinear heat capacity changes in glutamate dehydrogenase
  Biochemistry, 1986
• Temperature-dependent ΔC0p generated by a shift in equilibrium between macrostates of an enzyme
  Nature, 1981
• The Thermodynamics of Nucleotide Binding to Protein
  Critical Reviews in Biochemistry, 1980