Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Tobias Hüfner-Wulsdorf"'
Autor:
Tobias Hüfner-Wulsdorf, Gerhard Klebe
Publikováno v:
Journal of Chemical Information and Modeling. 60:6654-6665
Water molecules and their impact on the enthalpy and entropy of protein-ligand binding are of considerable interest in drug discovery. In this contribution, we use multiobjective optimization to fit the solvent enthalpy and entropy scoring terms of g
Autor:
F. Wieland Goetzke, Tobias Hüfner-Wulsdorf, François Diederich, Christoph Hohn, Klaus Reuter, F.R. Ehrmann, Maurice Sebastiani, Adrian Härtsch, E. Hassaan, Gerhard Klebe, Levon D. Movsisyan
Publikováno v:
Journal of Medicinal Chemistry, 63 (13)
Fragment-based lead discovery was applied to tRNA-guanine transglycosylase, an enzyme modifying post-transcriptionally tRNAs in Shigella, the causative agent of shigellosis. TGT inhibition prevents translation of Shigella's virulence factor VirF, hen
Autor:
Gerhard Klebe, Tobias Hüfner-Wulsdorf
Publikováno v:
Journal of Chemical Information and Modeling. 60:1818-1832
The mechanism by which water molecules modulate biomolecular interactions and the time scale of microscopic solvation processes are usually not known. This is particularly problematic as it prevents the incorporation of effects of water molecules int
Autor:
K. Ngo, Christoph P. Sager, Tobias Hüfner-Wulsdorf, Andreas Heine, Steffen Glöckner, Gerhard Klebe
Publikováno v:
ACS Chemical Biology. 15:675-685
Thermodynamics and kinetics of protein-ligand binding are both important aspects for the design of novel drug molecules. Presently, thermodynamic data are collected with isothermal titration calorimetry, while kinetic data are mostly derived from sur
Autor:
Gerhard Klebe, Tobias Hüfner-Wulsdorf
Publikováno v:
Journal of chemical information and modeling. 60(3)
In drug design, the importance of molecular solvation and desolvation is increasingly appreciated and water molecules are recognized as active contributors to protein-ligand binding. However, despite a number of theoretical approaches, computational
Publikováno v:
Journal of medicinal chemistry. 62(21)
Structural fixation of a ligand in its bioactive conformation may, due to entropic reasons, improve affinity. We present a congeneric series of thrombin ligands with a variety of functional groups triggering preorganization prior to binding. Fixation