This Review explores the dynamic behavior of water within nanopores and biological
channels in lipid bilayer membranes. We focus on molecular simulation studies, alongside …

Solid-state nuclear magnetic resonance (SSNMR) spectroscopy elucidates membrane
protein structures and dynamics in atomic detail to yield mechanistic insights. By …

Water-mediated interactions play key roles in drug binding. In protein sites with sparse polar
functionality, a small-molecule approach is often viewed as insufficient to achieve high …

Influenza A virus (IAV) matrix protein 2 (M2) is among the smallest bona fide, hence
extensively studied, ion channel proteins. The M2 ion channel activity is not only essential …

Mutation of the tumor suppressor gene, TP53, is associated with abysmal survival outcomes
in acute myeloid leukemia (AML). Although it is the most commonly mutated gene in cancer …

Abstract The influenza B M2 (BM2) proton channel is activated by acidic pH to mediate virus
uncoating. Unlike influenza A M2 (AM2), which conducts protons with strong inward …

The homotetrameric influenza A M2 channel (AM2) is an acid-activated proton channel
responsible for the acidification of the influenza virus interior, an important step in the viral …

Currently, completely abiotic channel systems that concurrently reproduce the high
selectivity and high permeation rate of natural protein channels are rare. Here, we provide …

High‐resolution crystal structures highlight the importance of water networks in protein–
ligand interactions. However, as these are typically determined at cryogenic temperature …

The M2 proton channel of influenza A is a drug target that is essential for the reproduction of
the flu virus. It is also a model system for the study of selective, unidirectional proton …