Browse our latest Structural Biology and Molecular Biophysics articles

A combined computational, genetic, and biochemical analysis of the hepatitis E virus open reading frame 1 (ORF1) protein identifies a novel domain-domain interaction that is vital for fitness and supports a proposed structural model of the ORF1 polyprotein.

Extremely significant interactions between α3-β7 and β12-α5 loops in the tetrameric L1 metallo-β-lactamase play an important role in the structural remodeling of the active site and offer insights into the potential for novel drug development by exploiting these interactions.

Photosystem II, the pigment-protein complex responsible for water oxidation in photosynthesis, was found to exist in two different core conformations with altered antennae connectivity.

Expression patterns and biophysical properties of acid-sensing ion channels in numerous bilaterian animals offer insight into the deployment of ion channels by the evolving nervous system in complex animals.

A theory is presented that explains why some ion channels tend to open in response to membrane stretching, which posits that channel closing is disfavored by the morphological energetics of the lipid bilayer, and increasingly so under lateral tension.

Combined patch-clamp fluorometry with ANAP, a fluorescent non-canonical amino acid, uncovers transitions in the activation pathway of human H_V1 that are modulated by voltage and the pH gradient.

The development of an integrative computational-experimental approach for identifying small molecules that can disrupt RNA:protein interactions in vitro and in cells led to the identification of several inhibitors of YBX1 in the micromolar range, including a previously approved drug.

SARS coronaviruses encode several mysterious proteins such as Orf3a and, in contrast to what has been claimed, Orf3a is not an ion channel but rather disrupts cellular trafficking by binding to the protein sorting complex known as HOPS.

A high-throughput analysis of several self-cleaving ribozymes reveals the effect of every possible mutation, and every possible pair of mutations, and how patterns in the relative activity data can be mapped to canonical and non-canonical structural elements.