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Servaas Michielssens
Researcher at Katholieke Universiteit Leuven
Publications - 19
Citations - 685
Servaas Michielssens is an academic researcher from Katholieke Universiteit Leuven. The author has contributed to research in topics: Dronpa & Hydrolysis. The author has an hindex of 10, co-authored 19 publications receiving 518 citations. Previous affiliations of Servaas Michielssens include Max Planck Society & Rega Institute for Medical Research.
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Journal ArticleDOI
Pmx: Automated protein structure and topology generation for alchemical perturbations.
TL;DR: This work presents an automated procedure to generate hybrid structures and topologies for the amino acid mutations in all commonly used force fields and says that the described software is compatible with the Gromacs simulation package.
Journal ArticleDOI
Accurate and Rigorous Prediction of the Changes in Protein Free Energies in a Large-Scale Mutation Scan.
TL;DR: This work achieves remarkable accuracy in a scan of 762 mutations estimating changes in protein thermostability based on the first principles of statistical mechanics, which enables accurate free‐energy estimates for diverse proteins, including the prediction of changes in the melting temperature of the membrane protein neurotensin receptor.
Book ChapterDOI
Calculation of binding free energies.
TL;DR: This chapter describes alchemical methods allowing the calculation of relative free energy differences using non-equilibrium approaches based on the Crooks Fluctuation Theorem, and provides a number of examples, including protein-ligand and protein-protein binding as well as ligand solvation free energy calculations.
Journal ArticleDOI
A designed conformational shift to control protein binding specificity.
Servaas Michielssens,Jan Peters,David Ban,Supriya Pratihar,Daniel Seeliger,Monika Sharma,Karin Giller,T. M. Sabo,Stefan Becker,Donghan Lee,Christian Griesinger,Bert L. de Groot +11 more
TL;DR: This work demonstrates how in silico designed point mutations within the core of ubiquitin, remote from the binding interface, change the binding specificity by shifting the conformational equilibrium of the ground-state ensemble between open and closed substates that have a similar population in the wild-type protein.
Journal ArticleDOI
Improved Replica Exchange Method for Native-State Protein Sampling.
TL;DR: The method was built upon the recently introduced replica exchange with solute tempering (REST), and the potential function is adapted to direct the conformational search toward interdomain movements and the flexible portions of the protein.