Browse our latest Structural Biology and Molecular Biophysics articles

Simulations of molecular dynamics suggest how the binding of the β-grasp domain of SUMO1 induces conformational and dynamic effects to activate SENP1.

DNA unwinding triggers a conformational change in the RecD subunit of E. coli RecBCD helicase-nuclease that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit.

Computations based on detailed atomic models explain how the ATP-driven sodium-potassium pump avoids transporting the wrong type of ions in order to maintain the physiological concentration of sodium and potassium ions across the cell membrane.

A human three-helix Rab-binding domain can potentially bind to two Rab proteins simultaneously with different affinities at binding sites generated by gene duplication.

The structure of the catalytic core of the N6-methyladenosine RNA methyltransferase complex METTL3-METTL14 reveals that METTL3 is the catalytic subunit, while METTL14 plays non-catalytic roles in substrate recognition and in maintaining complex integrity.

New biophysical methods and analyses visualize in real-time a chain of coordinated single-molecular events on a living cell, enabling the inner workings of a mechanoreceptor important to biology to be elucidated.

Components of a Spir:MyoV:Rab11 complex are recruited synergistically to coordinate actin tracks generation and myosin motor activity in vesicle transport processes.

Encapsulin-associated ferritin proteins form metal-dependent decamers that are active as ferroxidase enzymes, but require encapsulation to form an iron store.

Epigenetic modifications to DNA can regulate E3 ubiquitin ligase activity in human cells.

Measuring the equilibrium dimerization of a polytopic membrane protein in lipid bilayers forms the basis of a new system for studying the physical forces that stabilize membrane protein association in membranes.