Tunable intramolecular multicenter H-bonding interactions in first-row metal complexes bearing bidentate redox-active ligands.

In this research article, we report the synthesis and structural characterization of a family of first-row metal complexes bearing redox-active ligands with tunable H-bonding donors. We observed that these coordination complexes can adopt three different geometries and that they are stabilized by intramolecular multicenter H-bonding interactions, which are systematically modified by changing the metal ion (Co, Ni, Cu, Zn), the ligand scaffold (variations in the diamine and ureanyl substituents used) and the solvent of crystallization.

Catalytic Aerobic Oxidation of Alcohols by Copper Complexes Bearing Redox-Active Ligands with Tunable H-Bonding Groups.

In this research article, we describe the structure, spectroscopy, and reactivity of a family of copper complexes bearing bidentate redox-active ligands that contain H-bonding donor groups. Single-crystal X-ray crystallography shows that these tetracoordinate complexes are stabilized by intramolecular H-bonding interactions between the two ligand scaffolds. Interestingly, the Cu complexes undergo multiple reversible oxidation-reduction processes associated with the metal ion (Cu, Cu, Cu) and/or the o-phenyldiamido ligand (L, L, L).

Toward Computationally Designed Self-Reporting Biosensors Using Leave-One-Out Green Fluorescent Protein.

Leave-one-out green fluorescent protein (LOOn-GFP) is a circularly permuted and truncated GFP lacking the nth β-strand element. LOO7-GFP derived from the wild-type sequence (LOO7-WT) folds and reconstitutes fluorescence upon addition of β-strand 7 (S7) as an exogenous peptide. Computational protein design may be used to modify the sequence of LOO7-GFP to fit a different peptide sequence, while retaining the reconstitution activity.

Exploring the folding pathway of green fluorescent protein through disulfide engineering.

We have introduced two disulfide crosslinks into the loop regions on opposite ends of the beta barrel in superfolder green fluorescent protein (GFP) in order to better understand the nature of its folding pathway. When the disulfide on the side opposite the N/C-termini is formed, folding is 2× faster, unfolding is 2000× slower, and the protein is stabilized by 16 kJ/mol. But when the disulfide bond on the side of the termini is formed we see little change in the kinetics and stability.

THink: Inferring Cognitive Status from Subtle Behaviors.

The Digital Clock Drawing Test is a fielded application that provides a major advance over existing neuropsychological testing technology. It captures and analyzes high precision information about both outcome and process, opening up the possibility of detecting subtle cognitive impairment even when test results appear superficially normal. We describe the design and development of the test, document the role of AI in its capabilities, and report on its use over the past seven years.