Jennifer M. Johnston

TL;DR: Why protein-membrane hydrophobic matching is attained upon oligomerization at specific interfaces is shown from an analysis of coarse-grained molecular dynamics simulations of the spontaneous diffusion-interaction of the prototypical beta2-adrenergic (β2AR) receptors in a POPC lipid bilayer.

TL;DR: It is concluded that β1- and β2-adrenergic receptor homodimers with TM1/H8 at the interface are more stable than those involving TM4/3, and that this might be reconciled with experimental studies by considering a model of oligomerization in which more stable TM1 homodIMers diffuse through the membrane, transiently interacting with other protomers at interfaces involving other TM helices.

TL;DR: A concise overview of recent developments in computational biophysics of membrane proteins is provided, using GPCRs as an example to showcase important information that can be derived from modern MD simulations.

TL;DR: This work presents disulfide cross-linking experiments with DOR constructs with cysteines substituted at the extracellular ends of TM4 or TM5 that confirm the formation of DOR complexes involving these helices.

TL;DR: The kinetic properties of interfacial lipids are investigated, and their possible role in modulating the rate of receptor association and in promoting the formation of filiform aggregates is explored, thus supporting a distinctive role of the membrane in OR oligomerization and, possibly, signaling.