Scientists now have access to millions of accurate three-dimensional (3D) models of protein
structures. How do we leverage 3D structural models to learn about microbial functions …

Liquid–liquid phase separation of flexible biomolecules has been identified as a ubiquitous
phenomenon underlying the formation of membraneless organelles that harbor a multitude …

Glycans in the form of oligosaccharides, polysaccharides, and glycoconjugates are
ubiquitous in nature, and their structures range from linear assemblies to highly branched …

The dengue protease NS2B/NS3pro has been reported to adopt either an 'open'or a
'closed'conformation. We have developed a conformational filter that combines NMR with …

A novel spectroscopic approach for studying the flexibility and mobility in the hydrophobic
interior of lipid bilayers at specific depths is proposed. A set of test compounds featuring an …

The robustness of NMR coherence transfer in proximity of a paramagnetic center depends
on the relaxation properties of the nuclei involved. In the case of Iron-Sulfur Proteins …

Experimental NMR spectroscopy and theoretical molecular dynamics (MD) simulations
provide complementary insights into protein conformational dynamics and hence into …

We present an approach to optimize force field parameters using time-dependent data from
NMR relaxation experiments. To do so, we scan parameters in the dihedral angle potential …

Nuclear magnetic resonance (NMR) relaxation experiments shine light onto the dynamics of
molecular systems in the picosecond to millisecond timescales. As these methods cannot …

Nuclear magnetic resonance (NMR) spin relaxation is the most informative approach to
experimentally probe the internal dynamics of proteins on the picosecond to nanosecond …