Browse our latest Structural Biology and Molecular Biophysics articles

The X-ray crystal structure of the unusual carbon–carbon bond-forming biosynthetic enzyme CylK reveals a unique biochemical strategy for selective alkyl halide activation and substitution.

Deep mutagenesis experiments demonstrate that while cancer-causing mutations in Ras selectively alter regulatory interactions with GTPase-activating proteins, Ras is also activated by many mutations that decrease protein stability.

Advanced data analysis of molecular dynamics simulations of complex lipid membranes provides a quantitative and predictive model of the molecular features that control electroporation.

Surface plasmon resonance studies reveal that clustered protocadherins have precisely tuned trans homophilic binding interactions and promiscuous but variable cis interactions, consistent with the requirement of forming error-free linear molecular zippers used by mammalian neurons to distinguish self from nonself.

Cryo-EM structures of the eukaryotic clamp loader illustrate the large conformational changes that the clamp loader ATPase undergoes to open the circular sliding clamp and place it onto primer–template DNA.

A biochemical approach unveils the overall shape of a subclass of heavy-metal transporting pumps, thereby shedding light on principle molecular determinants linked to the transport mechanism of these elusive machines, information that is critical well beyond basic science.

A peptide toxin with therapeutic potential in stroke and pain induces multiple long-lasting conformational changes in acid-sensing ion channels and affects how the channels respond to endogenous ligands.

Through a single mutation at position 188, vertebrate rhodopsin acquires the ability to recover the dark state from the active state by a thermal reaction and by a photoreaction.

The Mg²⁺-channel CorA explores a wide conformational landscape of non-conducting states irrespective of bound Mg²⁺, but only in abscence of Mg²⁺, conducting states become accessible due to increased backbone dynamics.

Empirical energy landscape allows simulating the structural dynamics of the proteasomal ATPase complex, which yields predictions that are widely consistent with experimental observations and reveals the functional mechanism of the proteasome in substrate degradation.