Julian O. Streit

This study uses enhanced sampling simulations to explore the conformational space of Gaussia luciferase, revealing structural dynamics and substrate-binding features not captured by existing methods.

This study investigates the formation of the earliest structure during protein folding on the ribosome and identifies sub-ensembles that may facilitate co-translational folding.

This study structures two co-translational folding intermediates of an immunoglobulin-like domain using NMR and MD simulations, revealing parallel folding pathways conserved within the domain family.

This paper introduces OPES multithermal sampling to efficiently explore rare conformations in intrinsically disordered proteins, revealing transient tertiary structures in ACTR.

The paper introduces a benchmark for evaluating protein ensemble generators across ordered and disordered proteins and presents a new model that improves performance on disordered regions.

The paper investigates how protein conformational dynamics reveal hidden post-translational modification sites and their functional relevance across timescales.

This study identifies non-native amide-π interactions stabilizing a transient intermediate state in amyloid-forming human lysozyme using NMR and MD simulations.

This paper designs 19F NMR labels to improve chemical shift dispersion and enable structural analysis of proteins and their interactions.

The paper investigates the earliest steps of protein misfolding during alpha-1-antitrypsin biosynthesis, revealing co- and post-translational folding pathways and their implications for disease.

The paper uses structural biology techniques to study how nascent polypeptide chains fold through two distinct pathways during ribosome-mediated translation.

The paper shows that electrostatic repulsion between the ribosome and nascent proteins inhibits co-translational folding, with net charge being the main determinant of folding thermodynamics.

CryoENsemble improves conformational ensembles from molecular dynamics simulations to better match cryo-EM data and extract dynamics information.