Paramagnetic chemical probes have been used in electron paramagnetic resonance (EPR)
and nuclear magnetic resonance (NMR) spectroscopy for more than four decades. Recent …

Nuclear magnetic resonance (NMR) has long been instrumental in the characterization of
intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). This …

The AlphaFold Protein Structure Database contains predicted structures for millions of
proteins. For the majority of human proteins that contain intrinsically disordered regions …

Protein-protein interactions and the complexes thus formed are critical elements in a wide
variety of cellular events that require an atomic-level description to understand them in …

Transcription factors harbor defined regulatory intrinsically disordered regions (IDRs), which
raises the question of how they mediate binding to structured co-regulators and modulate …

Nuclear magnetic resonance (NMR) spectroscopy is a powerful method for studying the
structure and dynamics of proteins in their native state. For high-resolution NMR structure …

Solvent paramagnetic relaxation enhancement (sPRE) is a versatile nuclear magnetic
resonance (NMR)-based method that allows characterization of the structure and dynamics …

Transcription factor p53 protects cells against tumorigenesis when subjected to various
cellular stresses. Under these conditions, p53 interacts with transcription factor Forkhead …

Proteins and their interactions control a plethora of biological functions and enable life.
Protein–protein interactions can be highly dynamic, involve proteins with different degrees of …

The study of complex and dynamic biomolecular assemblies is a key challenge in structural
biology and requires the use of multiple methodologies providing complementary spatial …