The bacterial DNA sliding clamp, β-clamp: structure, interactions, dynamics and drug discovery.

DNA replication is a tightly coordinated event carried out by a multiprotein replication complex. An essential factor in the bacterial replication complex is the ring-shaped DNA sliding clamp, β-clamp, ensuring processive DNA replication and DNA repair through tethering of polymerases and DNA repair proteins to DNA. β -clamp is a hub protein with multiple interaction partners all binding through a conserved clamp binding sequence motif.

Checkpoint activation by Spd1: a competition-based system relying on tandem disordered PCNA binding motifs.

DNA regulation, replication and repair are processes fundamental to all known organisms and the sliding clamp proliferating cell nuclear antigen (PCNA) is central to all these processes. S-phase delaying protein 1 (Spd1) from S. pombe, an intrinsically disordered protein that causes checkpoint activation by inhibiting the enzyme ribonucleotide reductase, has one of the most divergent PCNA binding motifs known.

Identification of a Catalytic Nucleophile-Activating Network in the endoαAcetylgalactosaminidase of Family GH101.

endo-α--acetylgalactosaminidase (GH101), EngBF, is highly specific toward the mucin Core 1 glycan, Galβ1-3GalNAc. Apart from the side chains involved in the retaining mechanism of EngBF, Asp-682 is important for the activity. In the crystal structures of both EngBF and EngSP (from ), we identified a conserved water molecule in proximity to Asp-682 and the homologue residue in EngSP.

Experimental Reconstruction of the Few-Photon Nonlinear Scattering Matrix from a Single Quantum Dot in a Nanophotonic Waveguide.

Coherent photon-emitter interfaces offer a way to mediate efficient nonlinear photon-photon interactions, much needed for quantum information processing. Here we experimentally study the case of a two-level emitter, a quantum dot, coupled to a single optical mode in a nanophotonic waveguide. We carry out few-photon transport experiments and record the statistics of the light to reconstruct the scattering matrix elements of one- and two-photon components.

Effects of Cu(II) on the aggregation of amyloid-β.

Aberrant aggregation of the Aβ protein is a hallmark of Alzheimer's disease (AD), but no complete characterization of the molecular level pathogenesis has been achieved. A promising hypothesis is that dysfunction of metal ion homeostasis, and consequently, the undesired interaction of metal ions with Aβ, may be central to the development of AD. Qualitatively, most data indicate that Cu(II) induces rapid self-assembly of both Aβ40 and Aβ42 during the initial phase of the aggregation, while at longer time scales fibrillation may occur, depending on the experimental conditions.