A method for determining how many ions are required to drive transport in an electrogenic secondary active transporter will help understand the mechanisms of bacterial transporters whose structures have been solved.

The I_Ks potassium channel complex displays functional flexibility that depends on the ratio of its constituent KCNQ1 and KCNE1 protein subunits.

Building on previous work (Pless, 2013), we argue that side-chain 'flip out' is a key event in potassium channel C-type inactivation, and propose a new method for encoding multiple noncanonical amino acids and controlling protein stoichiometry.

A technology allows rapid screening of vast numbers of transcriptional factor combinatorials on stem cell programming.

In replicative ageing yeast cells, an age-dependent impediment in proper assembly of nuclear pore complexes is associated with altered nuclear transport.

Multimerization plays a functional role in EGFR activation and can be blocked by mutations in a specific region of Domain IV.

The mechanistic basis of molecular movement and interactions within plant root cells can be quantified using scanning fluorescence correlation spectroscopy.

The stoichiometry and mechanism of interactions of the Mis18 complex with M18BP1 was analysed to unveil the molecular basis of new CENP-A deposition during the G1 phase of the cell cycle.

A new technique called fastFISH enables nearly real-time and stoichiometric detection of nascent RNA and the tracking of individual stages of transcription at the level of single-molecules.

Quantitative observations of single-molecule binding between antigen and T cell receptor (TCR) in living primary T cells reveals unbinding kinetics, stoichiometry and signaling molecule recruitment, providing insights into the mechanisms of antigen recognition by the immune system.