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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Oligonucleotide Analogues with a Nucleobase‐Including Backbone, Part 7, Molecular Dynamics Simulation of a DNA Duplex Containing a 2′‐Deoxyadenosine 8‐(Hydroxymethyl)‐Derived Nucleotide
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Structure Determination of a Flexible Cyclic Peptide Based on NMR and MD Simulation 3J‐Coupling
TL;DR: Application of local-elevation search MD simulation in combination with biasing towards (3)J-coupling makes it possible to use (3]J-Couplings quantitatively in structure determination of peptides.
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On the use of a weak-coupling thermostat in replica-exchange molecular dynamics simulations.
TL;DR: This paper shows that an artifact in temperature replica-exchange molecular dynamics simulations in which the potential energy distributions appear not to be equal to the ones of standard MD simulations can be reduced or even eliminated by particular choices of the temperature coupling time of WC and the replica- Exchanges time period of T-REMD.
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Chemical library subset selection algorithms: A unified derivation using spatial statistics
TL;DR: The approach constitutes a unifying framework encompassing most proposed techniques as limiting cases and sheds light on their underlying assumptions, and vector quantization is obtained, in dimensions up to eight, in the limiting case of very smooth response surfaces for the integrated mean square error criterion.
Journal ArticleDOI
The key to predicting the stability of protein mutants lies in an accurate description and proper configurational sampling of the folded and denatured states.
Andreas P. Eichenberger,Wilfred F. van Gunsteren,Sereina Riniker,Lukas von Ziegler,Niels Hansen,Niels Hansen +5 more
TL;DR: The simulations may be used to link the structural Boltzmann ensembles to relative free enthalpies of folding between mutants and wild-type protein and show that unfolded conformations have to be treated with a sufficient level of detail in free energy calculations of protein stability.