Determination of Accurate Thermodynamics of Binding for Proteinase-Inhibitor Interactions

  • Frank Dullweber
  • Franz W. Sevenich
  • Gerhard Klebe

Abstract

The affinity of a low-molecular weight ligand to a macromolecular target protein is usually described by the binding constant Ki that typically corresponds to a negative free energy of binding of 10–80 kJ/mol in aqueous solution. It comprises enthalpic and entropie contributions that arise from several underlying phenomena. To better understand and subsequently describe the binding process detailed measurements of these quantities are required.

Keywords

Ethyl Enthalpy Titration Trypsin Calorimetry 

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Copyright information

© Springer Science+Business Media New York 2000

Authors and Affiliations

  • Frank Dullweber
    • 1
  • Franz W. Sevenich
    • 1
  • Gerhard Klebe
    • 1
  1. 1.Department of Pharmaceutical ChemistryPhilipps-Universität MarburgMarburgGermany

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