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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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Journal ArticleDOI
Interpreting NMR Data for β-Peptides Using Molecular Dynamics Simulations
TL;DR: NMR is one of the most used techniques to resolve structure of proteins and peptides in solution, however, inconsistencies may occur due to the fact that a polypeptide may adopt more than one confo...
Book ChapterDOI
Accounting for molecular mobility in structure determination based on nuclear magnetic resonance spectroscopic and X-ray diffraction data
Wilfred F. van Gunsteren,Roger M. Brunne,Piet Gros,RenéC Van Schaik,Celia A. Schiffer,Andrew E. Torda +5 more
TL;DR: This chapter discusses procedures to obtain an ideal representation of a biomolecule, with an eye to appropriately accounting for molecular mobility and flexibility in structure determination based on nuclear magnetic resonance (NMR) spectroscopic and x-ray diffraction data.
Journal ArticleDOI
Atomic Models of De Novo Designed ccβ-Met Amyloid-Like Fibrils
Michel O. Steinmetz,Zrinka Gattin,René Verel,Barbara Ciani,Thusnelda Stromer,Janelle M. Green,Peter Tittmann,Clemens Schulze-Briese,Heinz Gross,Wilfred F. van Gunsteren,Beat H. Meier,Louise C. Serpell,Shirley A. Müller,Richard A. Kammerer +13 more
TL;DR: The models provide a rational explanation why oxidation of methionine residues completely abolishes cc beta-Met amyloid fibril formation, indicating that a small number of site-specific hydrophobic interactions can play a major role in the packing of polypeptide-chain segments within amyloids fibrils.
Journal ArticleDOI
Molecular dynamics free energy calculation in four dimensions
TL;DR: In this paper, a new method for the calculation of free energy differences by molecular dynamics simulations of molecular systems is presented, where the main characteristic of the method is that the three-dimensional physical space is augmented by a further dimension.
Journal ArticleDOI
Peptide folding simulations: no solvent required?
TL;DR: In this article, the solvent degree of freedom of peptide and protein folding is explicitly treated in the atomic interaction function for a β-heptapeptide, and the results clearly show that the solvent cannot be ignored in folding simulations.