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

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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Détails bibliographiques
Auteur principal: Cramer, Jonathan
Autres auteurs: Klebe, Gerhard (Prof. Dr.) (Directeur de thèse)
Format: Dissertation
Langue:anglais
Publié: Philipps-Universität Marburg 2017
Sujets:
Thermodynamik
Thermodynamics
Thermolysin
Kinetik
Chemische Synthese
Phosphonamidat
Phosphonamidate
Synthesis
Wirkstoff
Kinetics
Synthese
Proteine
ITC
Bindungskinetik
Chemie
SPR
Chemistry & allied sciences
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Informations d'exemplaires de
Cote: urn:nbn:de:hebis:04-z2017-04658
Date de publication: 2018-08-08
Datum der Annahme: 2017-06-09
Downloads: 102 (2024), 99 (2023), 58 (2022), 37 (2021), 24 (2020), 36 (2019), 11 (2018)
Lizenz: https://rightsstatements.org/vocab/InC-NC/1.0/
URL d'accès: https://archiv.ub.uni-marburg.de/diss/z2017/0465
https://doi.org/10.17192/z2017.0465

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