Robert Scott Prosser

TL;DR: This work interrogated the functional, pharmacological, and biophysical properties of a GPCR, the β2-adrenergic receptor (β2AR), in high-density lipoprotein (HDL) particles and linked these functional differences in detergent- and HDL-reconstituted β2AR to a change in the equilibrium between inactive and active receptor states.

TL;DR: Current trends toward 19F-reporters that can be biosynthetically incorporated into proteins, and approaches to chemical tagging of proteins by 19F reporters are discussed, as well as improving delineation of states by 20F NMR.

TL;DR: It is shown that at high concentrations, a second substrate binds along the substrate-access channel of the occupied protomer, thereby dampening interprotomer dynamics and inhibiting catalysis, implying a role for the allosteric pocket at low substrate concentrations, where only a single substrate engages the enzyme at one time.

TL;DR: In this paper, 19F NMR can play a role in ascertaining activation mechanisms and understanding the complete energy landscape associated with signal transduction, and the chemical shift sensitivity of these reporters makes it possible to discern details of conformational ensembles.

TL;DR: It is proposed that labeling lysine side chains and N-terminal amino groups with indoles is a versatile and general strategy for bioconjugations with substituted indoles having broad implications for protein functionalization.