Progress toward the development of efficacious therapies for Alzheimer's disease (AD) is
halted by a lack of understanding early underlying pathological mechanisms. Systems …

Proteins are inherently flexible at ambient temperature. At equilibrium, they are
characterized by a set of conformations that undergo continuous exchange within a …

The p K a values and charge states of ionizable residues in polypeptides and proteins are
frequently determined via NMR-monitored pH titrations. To aid the interpretation of the …

Nuclear magnetic resonance (NMR) spectroscopy has evolved into a powerful tool for
fragment-based drug discovery over the last two decades. While NMR has been traditionally …

The characterization of the conformational properties of intrinsically disordered proteins
(IDPs), and their interaction modes with physiological partners has recently become a major …

Modern NMR spectroscopy has reached an unprecedented level of sophistication in the
determination of biomolecular structure and dynamics at atomic resolution in liquids …

Molecular Mechanics (MM) force fields are the methods of choice for protein simulations,
which are essential in the study of conformational flexibility. Given the importance of protein …

NMR spectroscopy is a key method for studying the structure and dynamics of (large)
multidomain proteins and complexes in solution. It plays a unique role in integrated …

This article gives an overview of some of the most recent trends in mass-spectrometry (MS)-
based approaches and their application in food metabolomics. MS is a powerful analytical …

Experimentally determined protein structures often feature missing domains. One example is
the C‐terminal domain (CTD) of the hepatitis B virus capsid protein, a functionally central …