Thanks to recent improvements in NMR spectrometer hardware and pulse sequence design,
modern 13C NMR has become a useful tool for biomolecular applications. The complete …

During the past decades, solution nuclear magnetic resonance (NMR) spectroscopy has
demonstrated itself as a promising tool in drug discovery. Especially, fragment-based drug …

Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a
stable three-dimensional structure, but rather adopt many different conformations in dynamic …

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

Many properties of intrinsically disordered proteins (IDPs), or protein regions (IDRs), are
modulated by the nature of amino acid side chains as well as by local solvent exposure. We …

Chemical denaturation is a well-established approach for probing the equilibrium between
folded and unfolded states of proteins. We demonstrate applicability of this method to the …

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 …

NMR spectroscopy is a particularly informative method for studying protein structures and
dynamics in solution; however, it is also one of the most time‐consuming. Modern …

Using SAXS and NMR spectroscopy, we herein provide a high-resolution description of the
intrinsically disordered N-terminal domain (PNT, aa 1–406) shared by the Nipah virus (NiV) …

The enhancement of nuclear relaxation rates due to the interaction with a paramagnetic
center (known as Paramagnetic Relaxation Enhancement) is a powerful source of structural …