Browse our latest Structural Biology and Molecular Biophysics articles

A comprehensive structural, biochemical, and cell biological analysis reveals the molecular mechanism and significance of the conserved interaction of centromeric protein N (CENP-N) with the centromeric nucleosome.

Understanding the structure of an antigen can guide the design of improved antigen-based vaccines.

Engineered E3 ubiquitin ligases are utilized to elucidate mechanisms underlying ubiquitin regulation of membrane proteins, and to achieve robust post-translational functional knockdown of ion channels.

Cryo-EM structures of actomyosin VI in multiple nucleotide states reveal a unique actin-myosin interface and a mechanism of force-sensitivity; furthermore, myosin VI remodels F-actin, suggesting a role for actin structural plasticity during force generation.

Structural, biochemical, and proteomic analyses of a four-subunit core module of the cleavage and polyadenylation specificity factor complex reveal its molecular architecture and specific determinants of polyadenylation signal recognition in human mRNAs.

Quantitative FRET UPR induction assay is used to measure IRE1 and BIP association and dissociation by a variety of ER misfolded proteins and by an important BiP substrate-binding domain mutant, significantly enhancing the evidence for the allosteric UPR induction model.

The antibody accessibility of the leptospiral surface protein, LigB, provides a guide for the rational design of improved recombinant chimeric vaccine antigens displayed on a single domain scaffold.

R788 is part of an allosteric communication pathway that connects the converter at the distal end of the myosin motor domain via the relay helix with switch-2 of the active site.

Cryo-EM reveals atomic details of two membrane half-channels for translocation of protons that drive rotary catalysis in ATP synthase.

The combination of high-speed light sheet microscopy and suitable data analysis facilitates cell-accurate measurements across entire organs and opens the way to systematic, scale-bridging, in vivo studies of organogenesis.