Protein stability is a topic of major interest for the biotechnology, pharmaceutical and food
industries, in addition to being a daily consideration for academic researchers studying …

Protein–ligand interactions are of fundamental importance in almost all processes in living
organisms. The ligands comprise small molecules, drugs or biological macromolecules and …

Chemical shifts contain important site-specific information on the structure and dynamics of
proteins. Deviations from statistical average values, known as random coil chemical shifts …

Inferring molecular structure from Nuclear Magnetic Resonance (NMR) measurements
requires an accurate forward model that can predict chemical shifts from 3D structure …

Intrinsically disordered proteins (IDPs) or regions of intrinsic disorder in otherwise folded
proteins (IDRs) play important roles in many different biological processes, including …

The prevalence of intrinsically disordered protein regions, particularly in eukaryotic proteins,
and their clear functional advantages for signaling and gene regulation have created an …

The phenomenon of chemical or conformational exchange in NMR spectroscopy has
enabled detailed characterization of time-dependent aspects of biomolecular function …

Disorder in proteins is vital for biological function, yet it is challenging to characterize.
Therefore, methods for predicting protein disorder from sequence are fundamental …

Intrinsically disordered proteins (IDPs) are often modeled using ideas from polymer physics
that suggest they smoothly explore all corners of configuration space. Experimental …

Traditionally, X-ray crystallography and NMR spectroscopy represent major workhorses of
structural biologists, with the lion share of protein structures reported in protein data bank …