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.
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Journal ArticleDOI
Biomolekulare Simulationen mit mehreren Auflösungsniveaus: ein Überblick über methodische Aspekte
Katharina Meier,Alexandra Choutko,Jozica Dolenc,Andreas P. Eichenberger,Sereina Riniker,Wilfred F. van Gunsteren +5 more
TL;DR: Theoretische and computer-gestutzte Modellierungen, die der Erklarung experimenteller Beobachtungen im Hinblick auf ein bestimmtes chemisches Phanomen oder einen bestimmten chemischen Prozess dienen, erfordern eine Reihe von Annahmen as discussed by the authors.
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On the use of one-step perturbation to investigate the dependence of NOE-derived atom-atom distance bound violations of peptides upon a variation of force-field parameters.
TL;DR: One-step perturbation constitutes an efficient technique to predict many values of different quantities from a single conformational ensemble for a particular system, which makes it a powerful force-field development technique that easily reduces the number of required separate simulations by an order of magnitude.
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Structure prediction of subtilisin BPN' mutants using molecular dynamics methods.
TL;DR: This paper compared the calculated structure of the mutants Met222Ala, Met222Phe and Met222Gln of subtilisin BPN' with the respective X-ray structures and found good agreement between predicted andX-ray structure.
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Exploring the effect of side-chain substitutions upon the secondary structure preferences of β-peptides.
TL;DR: Primary structure preferences of two sets of 16 β-peptides were investigated by means of one-step perturbation using molecular dynamics simulations and the results show that the substitution of a methyl group in the third or fourth residue stabilizes the left-handed 3(14)-helix over the right-handed 2.5(12-helix.
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Influence of 63Ser phosphorylation and dephosphorylation on the structure of the stathmin helical nucleation sequence: a molecular dynamics study.
TL;DR: The hypothesis of salt bridge derangement suggested by experimental observations of the stathmin nucleation sequence is extended, providing new insights into regulation of intrinsically disordered protein systems mediated by phosphorylation.