The all-atom additive CHARMM36 protein force field is widely used in molecular modeling
and simulations. We present its refinement, CHARMM36m (http://mackerell. umaryland …

Protein structure and dynamics can be characterized on the atomistic level with both nuclear
magnetic resonance (NMR) experiments and molecular dynamics (MD) simulations. Here …

The importance of Sulfur centred hydrogen bonds (SCHBs) cannot be underestimated given
the current day knowledge of its non-covalent interactions prevalent in many biopolymers as …

Peptide-based biomimetic catalysts are promising materials for efficient catalytic activity in
various biochemical transformations. However, their lack of operational stability and fragile …

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 …

Intramolecular NH… O, S, N interactions in non-tautomeric systems are reviewed in a broad
range of compounds covering a variety of NH donors and hydrogen bond acceptors. 1H …

Intrinsically disordered proteins (IDPs) represent a new frontier in structural biology since the
primary characteristic of IDPs is that structures need to be characterized as diverse …

Ion pairing is one of the most fundamental chemical interactions and is essential for
molecular recognition by biological macromolecules. From an experimental standpoint, very …

Dithioation of DNA phosphate is known to enhance binding affinities, at least for some
proteins. We mechanistically characterized this phenomenon for the Antennapedia …

Ion pairs (also known as salt bridges) of electrostatically interacting cationic and anionic
moieties are important for proteins and nucleic acids to perform their function. Although …