Browse our latest Structural Biology and Molecular Biophysics articles

Cell-penetrating peptide drugs prevent adrenergic regulation of pacemaker channels without altering the overall response of the cell to cAMP.

The complex process of protein translocation across membranes has been dissected into multiple key steps and the distributions of translocation rates indicate stochastic nature of the reaction.

A cryo-electron microscopy study of the human CLC-1 chloride ion channel reveals the structural basis of why some CLC proteins function as passive chloride channels whereas others function as an active proton-chloride antiporters.

A comprehensive approach to prediction of stabilizing mutations in G-protein coupled receptors yields high hit rate and crystal structures of 5HT2C in both active and inactive states.

Zebrafish genetics and cryo-electron tomography reveal distinct roles of all vertebrate PIH family proteins in axonemal dynein assembly and cilia/flagella motions, assigning specific dynein subtypes to each PIH protein.

Multi-body refinement in RELION allows high-resolution reconstruction and visualisation of molecular motions in cryo-EM single-particle data sets with continuous forms of structural heterogeneity.

Molecular insights to phytochrome activation and signal transduction over long distances enable the allosteric regulation of enzymatic effectors.

Temperature-activated TRPV1 ion channels respond to increased temperatures by opening and then entering an inactivated state from which they cannot recover, suggesting that this form of irreversible gating results from partial unfolding during heat absorption.

Fiducial-less tomography on single particle cryoEM samples reveals that most particles are adsorbed to the air-water interface and allows for researchers to diagnose and solve sample, grid, ice thickness, collection, and processing issues.

Antagonism between binding to unpolymerized subunits and to the lattice leads to a ratcheting model for the processive action of a microtubule polymerase.