H
H. Jelger Risselada
Researcher at University of Göttingen
Publications - 31
Citations - 7382
H. Jelger Risselada is an academic researcher from University of Göttingen. The author has contributed to research in topics: Membrane & Biology. The author has an hindex of 17, co-authored 21 publications receiving 6347 citations. Previous affiliations of H. Jelger Risselada include Leiden University & Max Planck Society.
Papers
More filters
Journal ArticleDOI
Efficient Quantification of Lipid Packing Defect Sensing by Amphipathic Peptides: Comparing Martini 2 and 3 with CHARMM36
TL;DR: An efficient end-state free energy calculation method is presented to quantify lipid packing defect sensing in molecular dynamics simulations and argues that these optimized defect sensors – aside from their biomedical and biophysical relevance – can provide valuable targets for the development of lipid force-fields.
Journal ArticleDOI
Martini 3: a coarse-grained force field with an eye for atomic detail.
TL;DR: The latest release of the popular and widely used force field for near-atomistic coarse-grained biomolecular simulations is presented.
Posted ContentDOI
Physics-based generative model of curvature sensing peptides; distinguishing sensors from binders
TL;DR: It is illustrated that sensing and binding are in fact phenomena that lie on the same thermodynamic contin-uum, with only subtle but explainable differences in membrane binding free energy, consistent with the serendipitous discovery of sensors.
Posted ContentDOI
Membrane interactions of mitochondrial lipid transfer proteins
Fereshteh Sadeqi,Kai Steffen Stroh,Marian Vache,Dietmar Riedel,Andreas Janshoff,H. Jelger Risselada,Michael Meinecke +6 more
TL;DR: It is shown that Ups1 interacts with membranes in a membrane curvature dependent manner and specifically binds to membrane regions where extraction and insertion of lipids is enhanced.
Journal ArticleDOI
Curvature model for nanoparticle size effects on peptide fibril stability and molecular dynamics simulation data
TL;DR: In this paper , a curvature model and molecular dynamics (MD) simulation data on the influence of nanoparticle size on the stability of amyloid peptide fibrils were presented.