71 research outputs found
Variations in the 6.2 m emission profile in starburst-dominated galaxies: a signature of polycyclic aromatic nitrogen heterocycles (PANHs)?
Analyses of the polycyclic aromatic hydrocarbon (PAH) feature profiles,
especially the 6.2 m feature, could indicate the presence of nitrogen
incorporated in their aromatic rings. In this work, 155 predominantly
starburst-dominated galaxies (including HII regions and Seyferts, for example),
extracted from the Spitzer/IRS ATLAS project (Hern\'an-Caballero &
Hatziminaoglou 2011), have their 6.2 m profiles fitted allowing their
separation into the Peeters' A, B and C classes (Peeters et al. 2002). 67% of
these galaxies were classified as class A, 31% were as class B and 2% as class
C. Currently class A sources, corresponding to a central wavelength near 6.22
m, seem only to be explained by polycyclic aromatic nitrogen heterocycles
(PANH, Hudgins et al. 2005), whereas class B may represent a mix between PAHs
and PANHs emissions or different PANH structures or ionization states.
Therefore, these spectra suggest a significant presence of PANHs in the
interstellar medium (ISM) of these galaxies that could be related to their
starburst-dominated emission. These results also suggest that PANHs constitute
another reservoir of nitrogen in the Universe, in addition to the nitrogen in
the gas phase and ices of the ISM
Comment on "Ab initio calculations of the lattice parameter and elastic stiffness coefficients of bcc Fe with solutes" Comp. Mat. Sci. v.126 pp.503-513 (2017)
In a recent paper, the authors propose to separately calculate the volumetric
and chemical contributions to the elastic stiffness coefficients of systems
containing solutes, as it is "computationally more efficient". We show that
this is not the case and further that their methodology and hence their results
are incorrect. There is no short cut for performing the desired calculations,
if done rigorously, as we show in our 2012 work
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Accurate Whole-Genome Sequencing and Haplotyping from 10 to 20 Human Cells
Recent advances in whole genome sequencing have brought the vision of personal genomics and genomic medicine closer to reality. However, current methods lack clinical accuracy and the ability to describe the context (haplotypes) in which genome variants co-occur in a cost-effective manner. Here we describe a low-cost DNA sequencing and haplotyping process, Long Fragment Read (LFR) technology, similar to sequencing long single DNA molecules without cloning or separation of metaphase chromosomes. In this study, ten LFR libraries were made using only ~100 pg of human DNA per sample. Up to 97% of the heterozygous single nucleotide variants (SNVs) were assembled into long haplotype contigs. Removal of false positive SNVs not phased by multiple LFR haplotypes resulted in a final genome error rate of 1 in 10 Mb. Cost-effective and accurate genome sequencing and haplotyping from 10-20 human cells, as demonstrated here, will enable comprehensive genetic studies and diverse clinical applications
Roadmap on photonic metasurfaces
Funding: C.R. and U.L. acknowledge support through the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy via the Excellence Cluster 3D Matter Made to Order (EXC-2082/1, Grant No. 390761711). A.B.E. acknowledges support through the Cluster of Excellence PhoenixD (EXC 2122, Project ID No. 390833453). I.F.-C. and C.R. acknowledge support through the CRC Waves: Analysis and Numerics (SFB 1173, Grant No. 258734477. K.A. acknowledges funding from the Swiss National Science Foundation (Project No. PZ00P2_193221).Here we present a roadmap on Photonic metasurfaces. This document consists of a number of perspective articles on different applications, challenge areas or technologies underlying photonic metasurfaces. Each perspective will introduce the topic, present a state of the art as well as give an insight into the future direction of the subfield.Peer reviewe
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A novel function of Rad54 protein - Stabilization of the Rad51 nucleoprotein filament
Homologous recombination is important for the repair of double-stranded DNA breaks in all organisms. Rad51. and Rad54 proteins are two key components of the homologous recombination machinery in eukaryotes. In vitro, Rad51. protein assembles with single-stranded DNA to form the helical nucleoprotein filament that promotes DNA strand exchange, a basic step of homologous recombination. Rad54 protein interacts with this Rad51. nucleoprotein filament and stimulates its DNA pairing activity, suggesting that Rad54 protein is a component of the nucleoprotein complex involved in the DNA homology search. Here, using physical criteria, we demonstrate directly the formation of Rad54-Rad51-DNA nucleoprotein co-complexes that contain equimolar amounts of each protein. The binding of Rad54 protein significantly stabilizes the Rad51 nucleoprotein filament formed on either single-stranded DNA or double-stranded DNA. The Rad54-stabilized nucleoprotein filament is more competent in DNA strand exchange and acts over a broader range of solution conditions. Thus, the co-assembly of an interacting partner with the Rad51. nucleoprotein filament represents a novel means of stabilizing the biochemical entity central to homologous recombination, and reveals a new function of Rad54 protein
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