United States Department of Energy

About: United States Department of Energy is a government organization based out in Washington D.C., District of Columbia, United States. It is known for research contribution in the topics: Coal & Catalysis. The organization has 13656 authors who have published 14177 publications receiving 556962 citations. The organization is also known as: DOE & Department of Energy.

Structures and dynamical properties of C n , Si n , Ge n , and Sn n clusters with n up to 13

Abstract: Car-Parrinello molecular dynamics simulated annealings were carried out for clusters ${\mathrm{Si}}_{n},$ ${\mathrm{Ge}}_{n},$ and ${\mathrm{Sn}}_{n}$ $(nl~13).$ We investigate the temperature regions in which these clusters transform from a ``liquidlike'' phase to a ``solidlike'' phase, and then from the ``solidlike'' phase to the ground-state structures. Additional simulated annealing was also performed for the cluster ${\mathrm{C}}_{13}$ which is selected as a prototype of small carbon clusters. In addition to the discovery of structures for Sn and Ge clusters, our simulation results also provide insights into the dynamics of cluster formation.

Metagenomic compendium of 189,680 DNA viruses from the human gut microbiome.

Abstract: Bacteriophages have important roles in the ecology of the human gut microbiome but are under-represented in reference databases. To address this problem, we assembled the Metagenomic Gut Virus catalogue that comprises 189,680 viral genomes from 11,810 publicly available human stool metagenomes. Over 75% of genomes represent double-stranded DNA phages that infect members of the Bacteroidia and Clostridia classes. Based on sequence clustering we identified 54,118 candidate viral species, 92% of which were not found in existing databases. The Metagenomic Gut Virus catalogue improves detection of viruses in stool metagenomes and accounts for nearly 40% of CRISPR spacers found in human gut Bacteria and Archaea. We also produced a catalogue of 459,375 viral protein clusters to explore the functional potential of the gut virome. This revealed tens of thousands of diversity-generating retroelements, which use error-prone reverse transcription to mutate target genes and may be involved in the molecular arms race between phages and their bacterial hosts.

The Orange Carotenoid Protein: a blue-green light photoactive protein

Abstract: This review focuses on the Orange Carotenoid Protein (OCP) which is the first photoactive protein identified containing a carotenoid as the photoresponsive chromophore. This protein is essential for the triggering of a photoprotective mechanism in cyanobacteria which decreases the excess absorbed energy arriving at the photosynthetic reaction centers by increasing thermal dissipation at the level of the phycobilisomes, the cyanobacterial antenna. Blue-green light causes structural changes within the carotenoid and the protein, converting the orange inactive form into a red active form. The activated red form interacts with the phycobilisome and induces the decrease of phycobilisome fluorescence emission and of the energy arriving to the photosynthetic reaction centers. The OCP is the light sensor, the signal propagator and the energy quencher. A second protein, the Fluorescence Recovery Protein (FRP), is needed to detach the red OCP from the phycobilisome and its reversion to the inactive orange form. In the last decade, in vivo and in vitro mechanistic studies combined with structural and genomic data resulted in both the discovery and a detailed picture of the function of the OCP and OCP-mediated photoprotection. Recent structural and functional results are emphasized and important previous results will be reviewed. Similarities to other blue-light responsive proteins will be discussed.