Inhibitor Synthesis and Biophysical Characterization of Protein–Ligand–Solvent Interactions An Analysis of the Thermodynamics and Kinetics of Ligand Binding to Thermolysin

Cramer, Jonathan

Inhibitor Synthesis and Biophysical Characterization of Protein–Ligand–Solvent Interactions An Analysis of the Thermodynamics and Kinetics of Ligand Binding to Thermolysin

In the pre-clinical development stages of most drug design campaigns, the equilibrium binding affinity of a prospective lead candidate, in the form of an IC50, Kd or ΔG° value, is the most commonly employed benchmark parameter for its effectiveness as a putative drug. Hydrogen bonding, van der Waals...

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Bibliografische gegevens
Hoofdauteur:	Cramer, Jonathan
Andere auteurs:	Klebe, Gerhard (Prof. Dr.) (Thesis begeleider)
Formaat:	Dissertation
Taal:	Engels
Gepubliceerd in:	Philipps-Universität Marburg 2017
Onderwerpen:	Thermodynamik Thermodynamics Thermolysin Kinetik Chemische Synthese Phosphonamidat Phosphonamidate Synthesis Wirkstoff Kinetics Synthese Proteine ITC Bindungskinetik Chemie SPR Chemistry & allied sciences
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Inhibitor Synthesis and Biophysical Characterization of Protein–Ligand–Solvent Interactions An Analysis of the Thermodynamics and Kinetics of Ligand Binding to Thermolysin

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