Browse our latest Structural Biology and Molecular Biophysics articles

Multi-site FRET measurements of moPrP oligomerization at low pH indicate that major conformational changes take place as monomers reversibly transform into large oligomers, which subsequently disassemble reversibly into small oligomers.

Single molecule subunit counting, FRET and electrophysiology experiments reveal that metabotropic glutamate receptor subunits interact and rearrange at the level of the transmembrane domains in response to allosteric modulators.

We are writing to comment on the article by El Hage et al., 2018 about molecular dynamics simulations of human hemoglobin.

We are writing to respond to the comment by Gapsys and de Groot, 2019 on our article about molecular dynamics simulations of human hemoglobin (El Hage et al., 2018).

First experimental studies on the ion atmosphere around a nucleosome provide a quantitative analysis of the molecule's electrostatic properties.

Cryo-EM reveals how the central functional site of the ribosome is assembled and provides a framework to interpret the consequences of mutations linked to leukaemia-associated ribosomopathies.

The ability to follow single objects in 3D in a living organism with high spatiotemporal resolution opens new possibilities for quantitative biophysical studies of complex systems in their physiological context.

Mass spectrometry analysis of purified pre-ribosomal RNAs shows that stable ribosomal RNA domains independently recruit assembly factors, and the cryo-EM structure of the 5' ETS ribonucleoprotein reveals regulatory conformational switches.

Cryo-electron microscopy reveals interactions at the interface between adeno-associated virus and its cellular receptor at 2.4Å resolution.

Two phosphorylation sites on 53BP1 are found to mediate interaction with TOPBP1-RAD9 and shown to be essential for assembling the G1 DNA damage checkpoint response apparatus.