Helmut Grubmüller

This paper assesses the accuracy of different force field combinations for simulating intrinsically disordered proteins and finds that combining C36m with OPC water improves accuracy for IDPs without compromising globular protein simulations.

This study shows that the Dam1 complex ring stabilizes kinetochore-microtubule attachments through a dynamic, disordered protein complex and microtubule structure, explaining force transduction and attachment stability.

The paper develops a minimal chemo-mechanical Markov model for F1-ATPase rotary catalysis, showing that four beta-subunit conformations are required and reconciling the bi-site versus tri-site controversy.

The paper identifies a bimodal distribution of peptide collision cross sections, showing two stable conformations, and proposes a two-valued predictor to improve peptide identification in proteomics.

The paper improves the conformational ensembles of folded proteins in GoMartini by optimizing G[o] networks using a perturbation-based approach against atomistic simulations.

The paper uses Bayesian Markov models to explain asymmetric ATP hydrolysis kinetics in ABCE1 without requiring direct cooperativity between nucleotide-binding sites.

The paper investigates the structure and function of otoferlin, showing how it binds Ca2+ and facilitates synaptic vesicle fusion in inner hair cells.

The paper shows UBE2J2 senses membrane lipid saturation by modulating its activity and interaction with E3 ligases, affecting ERAD ubiquitination.

The paper identifies transient non-local interactions in measles virus NTAIL that dominate its dynamics and regulate conformational preferences and function.

The paper analyzes a large peptide collisional cross section dataset to identify structural determinants of bimodal CCS behavior in peptides.

The paper characterizes the multi-timescale structural dynamics of the p53 transactivation domain using NMR and simulations, revealing a hierarchical energy landscape.

This study investigates how ULK1 activity influences ATG101 auto-activation dynamics, revealing a memory mechanism that accelerates autophagy complex formation.

This study shows that microtubule dynamics depend on the conformation and stability of clustered protofilaments, linking GTP hydrolysis to polymerization states.