W
Wilfred F. van Gunsteren
Researcher at École Polytechnique Fédérale de Lausanne
Publications - 427
Citations - 34308
Wilfred F. van Gunsteren is an academic researcher from École Polytechnique Fédérale de Lausanne. The author has contributed to research in topics: Molecular dynamics & Solvation. The author has an hindex of 86, co-authored 427 publications receiving 31426 citations. Previous affiliations of Wilfred F. van Gunsteren include University of Oxford & University of Groningen.
Papers
More filters
Journal ArticleDOI
Biomolecular simulation : historical picture and future perspectives
TL;DR: Bomolecular simulation may be used to interpret experimental data, to provoke new experiments, to replace experiments and to protect intellectual property.
Journal ArticleDOI
Computational Analysis of the Mechanism and Thermodynamics of Inhibition of Phosphodiesterase 5A by Synthetic Ligands.
TL;DR: This study looks at the mechanism and thermodynamics of the binding of selective inhibitors sildenafil and vardenafil to PDE5 using molecular dynamics simulations and focuses on critical evaluation of the SSP technique and the effects of computational parallelization on the efficiency of the technique.
Journal ArticleDOI
Peptidfaltung: Wenn die Simulation das Experiment erreicht
Xavier Daura,Karl Gademann,Bernhard Jaun,Dieter Seebach,Wilfred F. van Gunsteren,Alan E. Mark +5 more
TL;DR: In this article, akkurate Reproduktion des Mechanismus der reversiblen Peptidfaltung in Losung sowie von Konformationsunterschieden als Funktion der Aminosaurensequenz ermoglichen Molekuldynamik-Simulationen bei atomarer Auflosung.
Journal ArticleDOI
Peptides of Aminoxy Acids: A Molecular Dynamics Simulation Study of Conformational Equilibria under Various Conditions
TL;DR: This simulation shows the influence of temperature, type of solvent, and chain lengthening on the conformational behavior of peptide analogues formed by α-aminoxy acids as well as the total number of residues in the molecule.
Journal ArticleDOI
Refinement of the application of the GROMOS 54A7 force field to β‐peptides
TL;DR: The free enthalpy difference between the two helices is investigated as a function of a variation of different subsets of force‐field parameters to suggest that the disagreement with the experimental NMR data when using the 54A7 force field is caused by the use for β‐peptides of the new backbone φ‐/ψ‐torsional‐angle energy terms introduced in this force field.