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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.
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Molecular dynamics simulations of small peptides: can one derive conformational preferences from ROESY spectra?
Christine Peter,Magnus Rueping,Hans Jakob Wörner,Bernhard Jaun,Dieter Seebach,Wilfred F. van Gunsteren +5 more
TL;DR: Back-calculation of (1)H ROESY spectra and (3)J coupling constants from the MD simulations and comparison with the experimental data for the Val-Phe dipeptides shows good agreement between simulation and experiment, and reveals possible problems and pitfalls, when deriving structural properties of a small and extremely flexible molecule from NMR data only.
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Cooperative effects in the transport of small molecules through an amorphous polymer matrix
TL;DR: This article investigates a jump event in detail and employs both traditional molecular graphics techniques to show atomic motion and surface rendering methods to display the redistribution of penetrant-accessible volume in the polymer.
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Protein under pressure: molecular dynamics simulation of the arc repressor.
TL;DR: A tendency of conversion of intermolecular into intramolecular hydrogen bonds in the β‐sheet region has been detected, supporting the mentioned hypothesis and identifying the major structural and dynamical changes of the protein under such conditions.
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A comparison of methods for calculating NMR cross-relaxation rates (NOESY and ROESY intensities) in small peptides
TL;DR: The work shows that single conformations or a limited ensemble of configurations are insufficient to properly describe the behavior of the peptide and that different approaches to incorporate molecular motions lead to significant differences in the cross-relaxation rates calculated.
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Catalytic mechanism of cyclophilin as observed in molecular dynamics simulations: Pathway prediction and reconciliation of X-ray crystallographic and NMR solution data
TL;DR: The simulated N‐terminal rotated trans structure shows good agreement with the equivalent crystal structure and is consistent with the NMR data, illustrating the use of MD simulation at atomic resolution to model structural transitions and to interpret experimental data.