Molecular simulations, small-angle X-ray and neutron scattering experiments and previously measured NMR experiments were combined to study the structure and dynamics of the proteins and lipids in a nanodisc.
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.
Postsynaptic MT1-MMP serves as a molecular switch to synaptogenesis by clearing the surrounding ECM environment that allows effective deposition of nerve-derived synaptogenic factors to induce postsynaptic differentiation at developing NMJs.
Generation of a highly deuterated 13C-methyl labeled wild-type GPCR sample is used to facilitate characterization of the molecular environments and fast ps-ns dynamics of sidechains when the receptor is bound to ligands of different efficacy.
Nuclear magnetic resonance analysis revealed the structural and dynamical changes in MgtE during the channel closure caused by the cooperative Mg2+-binding, which had remained undescribed only by a static crystal structure.