51,042 research outputs found
COSMOGRAIL XVIII: time delays of the quadruply lensed quasar WFI2033-4723
We present new measurements of the time delays of WFI2033-4723. The data sets
used in this work include 14 years of data taken at the 1.2m Leonhard Euler
Swiss telescope, 13 years of data from the SMARTS 1.3m telescope at Las
Campanas Observatory and a single year of high-cadence and high-precision
monitoring at the MPIA 2.2m telescope. The time delays measured from these
different data sets, all taken in the R-band, are in good agreement with each
other and with previous measurements from the literature. Combining all the
time-delay estimates from our data sets results in Dt_AB = 36.2-0.8+0.7 days
(2.1% precision), Dt_AC = -23.3-1.4+1.2 days (5.6%) and Dt_BC = -59.4-1.3+1.3
days (2.2%). In addition, the close image pair A1-A2 of the lensed quasars can
be resolved in the MPIA 2.2m data. We measure a time delay consistent with zero
in this pair of images. We also explore the prior distributions of microlensing
time-delay potentially affecting the cosmological time-delay measurements of
WFI2033-4723. There is however no strong indication in our measurements that
microlensing time delay is neither present nor absent. This work is part of a
H0LiCOW series focusing on measuring the Hubble constant from WFI2033-4723.Comment: Submitted to Astronomy and Astrophysic
A model of large-scale proteome evolution
The next step in the understanding of the genome organization, after the
determination of complete sequences, involves proteomics. The proteome includes
the whole set of protein-protein interactions, and two recent independent
studies have shown that its topology displays a number of surprising features
shared by other complex networks, both natural and artificial. In order to
understand the origins of this topology and its evolutionary implications, we
present a simple model of proteome evolution that is able to reproduce many of
the observed statistical regularities reported from the analysis of the yeast
proteome. Our results suggest that the observed patterns can be explained by a
process of gene duplication and diversification that would evolve proteome
networks under a selection pressure, favoring robustness against failure of its
individual components
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