Bending nanofibers into nanospirals: coordination chemistry as a tool for shaping hydrophobic assemblies.

In the current work, we demonstrate how coordination chemistry can be employed to direct self-assembly based on strong hydrophobic interactions. To investigate the influence of coordination sphere geometry on aqueous self-assembly, we synthesized complexes of the amphiphilic perylene diimide terpyridine ligand with the first-row transition-metal centers (zinc, cobalt, and nickel). In aqueous medium, aggregation of these complexes is induced by hydrophobic interactions between the ligands.

A programmable biomolecular computing machine with bacterial phenotype output.

The main advantage of autonomous biomolecular computing devices over electronic computers is their ability to interact directly with biological systems. No interface is required since all components of molecular computers, including hardware, software, input, and output are molecules that interact in solution along a cascade of programmable chemical events. Here, we demonstrate for the first time that the output of a computation preduced by a molecular finite automaton can be a visible bacterial phenotype.

Parallel biomolecular computation on surfaces with advanced finite automata.

A biomolecular, programmable 3-symbol-3-state finite automaton is reported. This automaton computes autonomously with all of its components, including hardware, software, input, and output being biomolecules mixed together in solution. The hardware consisted of two enzymes: an endonuclease, BbvI, and T4 DNA ligase.

Pi-accepting-pincer rhodium complexes: an unusual coordination mode of PCP-type systems.

The novel pi-accepting, pincer-type ligand, dipyrrolylphoshinoxylene (DPyPX), is introduced. This ligand has the strongest pi-accepting phosphines used so far in the PCP family of ligands and this results in some unusual coordination chemistry. The rhodium(I) complex, [(DPyPX)Rh(CO)(PR3)] (4, R=Ph, Et, pyrrolyl) is prepared by treating the relevant [(DPyPX)Rh(PR3)] (3) complex with CO and is remarkably resistant to loss of either ligand.

Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression.

Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation.