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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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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Plaatsingsnummer: urn:nbn:de:hebis:04-z2017-04658
Publicatiedatum: 2018-08-08
Datum der Annahme: 2017-06-09
Downloads: 97 (2024), 99 (2023), 58 (2022), 37 (2021), 24 (2020), 36 (2019), 11 (2018)
Lizenz: https://rightsstatements.org/vocab/InC-NC/1.0/
URL naar item: https://archiv.ub.uni-marburg.de/diss/z2017/0465
https://doi.org/10.17192/z2017.0465

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