Browse our latest Structural Biology and Molecular Biophysics articles

Protein kinase dysregulation, implicated in various diseases via cell signaling pathways, can be therapeutically and experimentally managed through allosteric modulation, facilitated by a dynamic network of interactions, with computational techniques enabling precise control in live systems.

A comprehensive computational study of germline-encoded T cell receptor CDR loops and MHC alpha-helices finds limited evidence for evolutionary conserved interactions, and instead suggests broad biophysical compatibility guides the interactions between the two proteins.

Structural analysis of the HipBST toxin–antitoxin system from E. coli shows how a toxin kinase has been split into two proteins and encodes its own inhibitor.

The sensory regulatory system of the cholera causative involves the detection of bile acids by direct interaction with the inner membrane protein complex formed by ToxR and ToxS, thereby inducing concentration-dependent structural changes.

The disease-associated aggregation of polyglutamine begins in a single molecule with a specific structure.

The cellular membrane competes with Abl for myristoyl binding to stabilize the preactivated state and enhance allosteric activation.

A structural and biochemical study reveals the molecular mechanism of the predator–prey associations of Aplysia kurodai and brown algae (akuBGL–phlorotannin/laminarin–EHEP system), which has high-potential applications in the biotechnology industry.

Modular folding of kinesin-1 motor proteins enables a fully autoinhibited state.

Cryo-EM, Molecular Dynamics, and in vitro binding assays are combined to elucidate a new occluded conformation associated with zinc binding and energy coupling with the proton motive force.

Sea anemones use adapted ion channels to control stinging behavior.