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.

A variable number of auxiliary subunit molecules (TARPs) accompanying AMPARs have a differential impact on channel behavior showing also striking differences between AMPAR subtypes.

Stoichiometric interactions between microtubules and cortical force-generators set spindle size, position and dynamics, and its scaling with cell size in nematode species.

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.

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

NHE1-CaM complexes of multiple stoichiometries regulate cellular Ca²⁺-dependent NHE1 activity and can contribute to NHE1 dimerization, the latter shown by the NMR structure of CaM linking two NHE1 cytosolic tails.

An in vitro reconstitution assay reveals stoichiometric levels of the short form of Opa1 work together with the long form of Opa1 to mediate efficient and fast membrane pore opening.

The high affinity α-synuclein-monomer binder AS69 converts into a strong sub-stoichiometric inhibitor of nucleation processes upon formation of the AS69-α-synuclein complex, achieving reduced aggregation in vitro and in vivo.

Crystal structures provide structural rationales for the transport stoichiometry of the gastric proton pump, which suffices the energy requirement for the generation of a million-fold proton gradient across the membrane.