Terrestrial Consequences of Spectral and Temporal Variability in Ionizing Photon Events

Gamma-Ray Bursts (GRBs) directed at Earth from within a few kpc may have damaged the biosphere, primarily though changes in atmospheric chemistry which admit greatly increased Solar UV. However, GRBs are highly variable in spectrum and duration. Recent observations indicate that short (~0.1 s) burst GRBs, which have harder spectra, may be sufficiently abundant at low redshift that they may offer an additional significant effect. A much longer timescale is associated with shock breakout luminosity observed in the soft X-ray (~10^3 s) and UV (~10^5 s) emission, and radioactive decay gamma-ray line radiation emitted during the light curve phase of supernovae (~10^7 s). Here we generalize our atmospheric computations to include a broad range of peak photon energies and investigate the effect of burst duration while holding total fluence and other parameters constant. The results can be used to estimate the probable impact of various kinds of ionizing events (such as short GRBs, X-ray flashes, supernovae) upon the terrestrial atmosphere. We find that the ultimate intensity of atmospheric effects varies only slightly with burst duration from 10^-1 s to 10^8 s. Therefore, the effect of many astrophysical events causing atmospheric ionization can be approximated without including time development. Detailed modeling requires specification of the season and latitude of the event. Harder photon spectra produce greater atmospheric effects for spectra with peaks up to about 20 MeV, because of greater penetration into the stratosphere.Comment: 30 pages, to be published in ApJ. Replaced for conformity with published version, including correction of minor typos and updated reference

BioTIME: A database of biodiversity time series for the Anthropocene.

MotivationThe BioTIME database contains raw data on species identities and abundances in ecological assemblages through time. These data enable users to calculate temporal trends in biodiversity within and amongst assemblages using a broad range of metrics. BioTIME is being developed as a community-led open-source database of biodiversity time series. Our goal is to accelerate and facilitate quantitative analysis of temporal patterns of biodiversity in the Anthropocene.Main types of variables includedThe database contains 8,777,413 species abundance records, from assemblages consistently sampled for a minimum of 2 years, which need not necessarily be consecutive. In addition, the database contains metadata relating to sampling methodology and contextual information about each record.Spatial location and grainBioTIME is a global database of 547,161 unique sampling locations spanning the marine, freshwater and terrestrial realms. Grain size varies across datasets from 0.0000000158 km2 (158 cm2) to 100 km2 (1,000,000,000,000 cm2).Time period and grainBioTIME records span from 1874 to 2016. The minimal temporal grain across all datasets in BioTIME is a year.Major taxa and level of measurementBioTIME includes data from 44,440 species across the plant and animal kingdoms, ranging from plants, plankton and terrestrial invertebrates to small and large vertebrates.Software format.csv and .SQL

Scientific Assessment of Climate Change and Its Effects in Maine

Climate change has already made its presence known in Maine, from shorter winters and warmer summers with ocean heat waves, to stronger storms, new species showing up in our backyards and the Gulf of Maine, aquatic algal blooms, acidic ocean waters that affect shellfish, and new pests and diseases that harm our iconic forests and fisheries. The health of Maine people is also being affected by climate change, from high heat index days driving increased emergency room visits to the ravages of Lyme and other vector-borne diseases. And our economy is feeling the effects, too — with farmers trying to adapt to longer growing seasons but dealing with severe storms and late frosts, aquaculturists already adapting to a more acidic ocean, and winter sports like skiing and snowmobiling being impacted by our shrinking winter season. This is the first report from the Maine Climate Council’s Scientific and Technical Subcommittee, produced by more than 50 scientists from around the State representing Scientific and Technical Subcommittee members, other co-authors, and contributors. This report is part of the 2020 Maine Climate Action Plan. The report summarizes how climate change has already impacted Maine and how it might continue affecting our State in the future

Species richness in North Atlantic fish: Process concealed by pattern

International audiencePrevious analyses of marine fish species richness based on presence‐absence data have shown changes with latitude and average species size, but little is known about the underlying processes. To elucidate these processes we use metabolic, neutral and descriptive statistical models to analyse how richness responds to maximum species length, fish abundance, temperature, primary production, depth, latitude and longitude, while accounting for differences in species catchability, sampling effort and mesh size

A facile strategy for the modification of polyethylene substrates with non-fouling, bioactive poly(poly(ethylene glycol) methacrylate) brushes

This manuscript reports a facile strategy for the modification of polyethylene, a widely used biomaterial, with a thin non-biofouling coating that can act as a platform to introduce biochemical cues to control and direct, e.g., cell adhesion and proliferation. The non-biofouling coating is produced, following a two-step strategy involving photobromination of the polyethylene substrate followed by surface-initiated ATRP of poly(ethylene glycol) methacrylate. The resulting coatings, which are referred to as polymer brushes, are robust and withstand prolonged exposure to aqueous ethanol and phosphate buffered saline and also do not show any signs of detachment or degradation in the in vivo studies over a period of 10 d. Functionalization of these polymer brush coatings with extracellular matrix derived peptide sequences, promotes adhesion and spreading of endothelial cells

Different Dark Conformations Function in Color-Sensitive Photosignaling by the Sensory Rhodopsin I-HtrI Complex

The haloarchaeal phototaxis receptor sensory rhodopsin I (SRI) in complex with its transducer HtrI delivers an attractant signal from excitation with an orange photon and a repellent signal from a second near-UV photon excitation. Using a proteoliposome system with purified SRI in complex with its transducer HtrI, we identified by site-directed fluorescence labeling a site (Ser155) on SRI that is conformationally active in signal relay to HtrI. Using site-directed spin labeling of Ser155Cys with a nitroxide side chain, we detected a change in conformation following one-photon excitation such that the spin probe exhibits a splitting of the outer hyperfine extrema (\documentclass[10pt]{article} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{pmc} \pagestyle{empty} \oddsidemargin -1.0in \begin{document} \begin{equation*}2{\mathrm{A^{\prime}_{zz}}}\end{equation*}\end{document}) significantly smaller than that of the electron paramagnetic resonance spectrum in the dark state. The dark conformations of five mutant complexes that do not discriminate between orange and near-UV excitation show shifts to lower or higher \documentclass[10pt]{article} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{pmc} \pagestyle{empty} \oddsidemargin -1.0in \begin{document} \begin{equation*}2{\mathrm{A^{\prime}_{zz}}}\end{equation*}\end{document} values correlated with the alterations in their motility behavior to one- and two-photon stimuli. These data are interpreted in terms of a model in which the dark complex is populated by two conformers in the wild type, one that inhibits the CheA kinase (A) and the other that activates it (R), shifted in the dark by mutations and shifted in the wild-type SRI-HtrI complex in opposite directions by one-photon and two-photon reactions

Viewing rare conformations of the β2 adrenergic receptor with pressure-resolved DEER spectroscopy

The β2 adrenergic receptor (β2AR) is an archetypal G protein coupled receptor (GPCR). One structural signature of GPCR activation is a large-scale movement (ca. 6 to 14 Å) of transmembrane helix 6 (TM6) to a conformation which binds and activates a cognate G protein. The β2AR exhibits a low level of agonist-independent G protein activation. The structural origin of this basal activity and its suppression by inverse agonists is unknown but could involve a unique receptor conformation that promotes G protein activation. Alternatively, a conformational selection model proposes that a minor population of the canonical active receptor conformation exists in equilibrium with inactive forms, thus giving rise to basal activity of the ligand-free receptor. Previous spin-labeling and fluorescence resonance energy transfer experiments designed to monitor the positional distribution of TM6 did not detect the presence of the active conformation of ligand-free β2AR. Here we employ spin-labeling and pressure-resolved double electron-electron resonance spectroscopy to reveal the presence of a minor population of unliganded receptor, with the signature outward TM6 displacement, in equilibrium with inactive conformations. Binding of inverse agonists suppresses this population. These results provide direct structural evidence in favor of a conformational selection model for basal activity in β2AR and provide a mechanism for inverse agonism. In addition, they emphasize 1) the importance of minor populations in GPCR catalytic function; 2) the use of spin-labeling and variable-pressure electron paramagnetic resonance to reveal them in a membrane protein; and 3) the quantitative evaluation of their thermodynamic properties relative to the inactive forms, including free energy, partial molar volume, and compressibility

Ligand efficacy modulates conformational dynamics of the µ-opioid receptor

The µ-opioid receptor (µOR) is an important target for pain management1 and molecular understanding of drug action on µOR will facilitate the development of better therapeutics. Here we show, using double electron–electron resonance and single-molecule fluorescence resonance energy transfer, how ligand-specific conformational changes of µOR translate into a broad range of intrinsic efficacies at the transducer level. We identify several conformations of the cytoplasmic face of the receptor that interconvert on different timescales, including a pre-activated conformation that is capable of G-protein binding, and a fully activated conformation that markedly reduces GDP affinity within the ternary complex. Interaction of β-arrestin-1 with the μOR core binding site appears less specific and occurs with much lower affinity than binding of Gi