Browse our latest Structural Biology and Molecular Biophysics articles

UV-Vis- and IR-spectroscopy provides insights into the light-induced enzyme activity of a rhodopsin guanylyl cyclase by tracking the substrate turnover with atomic resolution in real-time and correlating it with the structural changes of the protein.

Mechanically activated Piezo1 ion channels, at physiologically relevant densities, behave as independent mechanotransducers, which we propose is essential for homogenous transduction of forces across the entire cell membrane.

Fibrinogen, a key protein involved in blood coagulation, contains a disordered and previously poorly characterised region called αC that plays a critical role in fibrin fibre growth and clot stability.

Fluorescence fluctuation spectroscopy is implemented for detection of up to four molecular species, allowing users to quantify molecular interactions and stoichiometry of multicomponent complexes in live cells, in a wide range of biological processes, from membrane signaling to viral assembly.

Single-molecule fluorescence experiments reveal transcription initiation proceeds via a 'bind-unwind-load-and-lock' mechanism where promoter DNA unwinds outside the RNA polymerase (RNAP) cleft, the unwound template-DNA loads into the cleft, and RNAP 'locks' the template-DNA by closing the RNAP clamp module.

Quantitative FRET imaging in moving C. elegans shows that stretch-unfolding of twitchin kinase occurs in the active muscle, whereby mechanical activity titrates the signaling pathway of this cytoskeletal kinase.

The structure of the Mycobacterium smegmatis CIII₂CIV₂ respiratory supercomplex with telacebec (Q203) bound shows how this tuberculosis drug candidate blocks respiration in mycobacteria.

The RNA-mediated higher order assembly of TDP-43, a protein associated with neurodegenerative diseases, preserves its solubility by reducing the risk of multivalent interactions between low complexity domains.

A pentameric channel-receptor was studied by combining allosteric mutations, electrophysiology, fluorescent reporters and normal mode analysis, to dissect the long-range allosteric couplings specifically involved in its pre-activation and activation.

Time-resolved transition metal ion fluorescence resonance energy transfer using a fluorescent, noncanonical amino acid donor and metal ion acceptor measures distances and distance distributions in proteins, allowing the equilibrium distributions among conformational states to be accurately determined.