Justin P. Gallivan

TL;DR: In this paper, an energy-based criterion for selecting significant sidechain pairs was used to identify and evaluate cation-pi interactions in protein structures, and it was clearly demonstrated that, when a cationic sidechain (Lys or Arg) is near an aromatic side chain (Phe, Tyr, or Trp), the geometry is biased toward one that would experience a favorable cationpi interaction.

TL;DR: This finding indicates that, on binding, the cationic, quaternary ammonium group of acetylcholine makes van der Waals contact with the indole side chain of alpha tryptophan-149, providing the most precise structural information to date on this receptor.

TL;DR: In this paper, a direct comparison of the energetic significance of a representative salt bridge vs a representative cation−π interaction in aqueous media and in a range of organic solvents is presented using ab initio electronic structures and the SM5.42R/HF solvation model of Cramer and Truhlar.

TL;DR: It is demonstrated that synthetic riboswitches that activate protein translation in response to a specific small molecule can be used to perform sensitive genetic screens and selections for the presence of small molecules in Escherichia coli and that the exquisite molecular discrimination properties of aptamers selected in vitro translate directly into an in vivo genetic selection system.

TL;DR: Continuing efforts focus on incorporating unnatural amino acids that differ substantially from the natural amino acids, for example, residues that include fluorophores, as well as addressing the feasibility of incorporating unnatural acids into ion channels and membrane receptors in mammalian cells.