Designing a reliable computational methodology to calculate protein: ligand standard
binding free energies is extremely challenging. The large change in configurational enthalpy …

Cation-π interactions arise as a result of strong attractive forces between positively charged
entities and the π-electron cloud of aromatic groups. The physicochemical characteristics of …

Various physics-and data-driven sequence-dependent protein coarse-grained models have
been developed to study biomolecular phase separation and elucidate the dominant …

Reproducing the structure and function of biological membrane channels, synthetic
nanopores have been developed for applications in membrane filtration technologies and …

Pentameric ligand-gated ion channels (pLGICs) mediate synaptic transmission and are
sensitive to their lipid environment. The mechanism of phospholipid modulation of any …

Intracellular condensates are highly multi-component systems in which complex phase
behaviour can ensue, including the formation of architectures comprising multiple …

Systematic and quantitative analysis of the reliability of formally exact methods that in silico
calculate absolute protein–ligand binding free energies remains lacking. Here, we provide …

The strongly attractive noncovalent interactions of charged atoms or molecules with π-
systems are important binding motifs in many chemical and biological systems. These so …

Aromatic residues can participate in various biomolecular interactions, such as π–π, cation−
π, and CH− π interactions, which are essential for protein structure and function. Here, we re …

The binding energies for cation− π complexation are underestimated by traditional fixed-
charge force fields owing to their lack of explicit treatment of ion-induced dipole interactions …