Partisanship and public opinion of COVID-19: Does emphasizing Trump and his administration’s response to the pandemic affect public opinion about the coronavirus?

This is the final version. Available on open access from Routledge via the DOI in this recordDoes emphasizing the pandemic as a partisan issue polarize factual beliefs, attitudes, and behavioral intentions concerning the SARS-CoV-2/COVID-19 pandemic? To answer this question, we conducted a preregistered survey experiment with a “questions as treatment” design in late March 2020 with 1,587 U.S. respondents recruited via Prime Panel. Respondents were randomly assigned to answer several questions about then-president Donald J. Trump and the coronavirus (including receiving an information cue by evaluating one of Trump’s tweets) either at the beginning of the survey (treated condition) or at the end of the survey (control condition). Receiving these questions at the beginning of the survey had no direct effect on COVID-19 factual beliefs, attitudes, and behavioral intentions.European Union Horizon 202

Dipolar relaxation in a lipid bilayer detected by a fluorescent probe, 4''-dimethylaminochalcone

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Public perceptions and misperceptions of political authority in the European Union

This is the author accepted manuscript.How do citizens understand political authority within multi-level systems? We use original survey data from six European Union member states to assess the roles of political identity and interest in shaping citizen attitudes towards political authority in the European Union. We find that citizens with a greater interest in politics are more likely to express views on the authority of the European Union. These individuals are less likely to be uninformed. Interest does not necessarily mean that individuals hold correct perceptions. A substantive amount of voters are misinformed about the power of Brussels. We find that citizens with an exclusively national identity are more likely to hold misperceptions than those who think of themselves as both members of their nation and as Europeans.European Union Horizon 202

Relation between pH, structure, and absorption spectrum of Cerulean: A study by molecular dynamics and TD DFT calculations

cited By 6International audienceMolecular dynamics (MD) and quantum mechanical calculations of the Cerulean green fluorescent protein (a variant of enhanced cyan fluorescent protein ECFP) at pH 5.0 and 8.0 are presented, addressing two questions arising from experimental results (Malo et al., Biochemistry 2007;46:9865 - 9873): the origin of the blue shift of absorption spectrum when the pH is decreased from 8.0 to 5.0, and the lateral chain orientation of the key residue Asp 148. We demonstrate that the blue shift is reproduced assuming that a rotation around the single bond of the exocydie ring of the chromophore takes place when the pH changes from 5.0 to 8.0. We find that Asp 148 is protonated and inside the barrel at pH 5.0 in agreement with crystallographic data. However, the hydrogen bond pattern of Asp 148 is different in simulations of the solvated protein and in the crystal structure. This difference is explained by a partial closing of the cleft between strands 6 and 7 in MD simulations. This study provides also a structure at pH 8.0: the Asp 148 carboxylate group is exposed to the solvent and the chromophore is stabilized in the trans conformation by a tighter hydrogen bond network. This work gives some insight into the relationship between the pH and the chromophore conformation and suggests an interpretation of the very similar fluorescent properties of ECFP and ECFP/ H148D

Excited state dynamics of the green fluorescent protein on the nanosecond time scale

cited By 18International audienceWe have introduced a new algorithm in the parallel processing PMEMD module of the AMBER suite that allows MD simulations with a potential involving two coupled torsions. We have used this modified module to study the green fluorescent protein. A coupled torsional potential was adjusted on high accuracy quantum chemical calculations of the anionic chromophore in the first excited state, and several 15-ns-long MD simulations were performed. We have obtained an estimate of the fluorescence lifetime (2.2 ns) to be compared to the experimental value (3 ns), which is, to the best of our knowledge, the first theoretical estimate of that lifetime

Complex fluorescence of the cyan fluorescent protein: Comparisons with the H148D variant and consequences for quantitative cell imaging

cited By 37International audienceWe have studied the fluorescence decays of the purified enhanced cyan fluorescent protein (ECFP, with chromophore sequence Thr-Trp-Gly) and of its variant carrying the single H148D mutation characteristic of the brighter form Cerulean. Both proteins exhibit highly complex fluorescence decays showing strong temperature and pH dependences. At neutral pH, the H148D mutation leads (i) to a general increase in all fluorescence lifetimes and (ii) to the disappearance of a subpopulation, estimated to be more than 25% of the total ECFP molecules, characterized by a quenched and red-shifted fluorescence. The fluorescence lifetime distributions of ECFP and its H148D mutant remain otherwise very similar, indicating a high degree of structural and dynamic similarity of the two proteins in their major form. From thermodynamic analysis, we conclude that the multiexponential decay of ECFP cannot be simply ascribed, as is generally admitted, to the slow conformational exchange characterized by NMR and X-ray crystallographic studies [Seifert, M. H., et al. (2002) J. Am. Chem. Soc. 124, 7932-7942; Bae, J. H., et al. (2003) J. Mol. Biol. 328, 1071-1081]. Parallel measurements in living cells show that these fluorescence properties in neutral solution are very similar to those of cytosolic ECFP

Natural Genetic Transformation: A Direct Route to Easy Insertion of Chimeric Genes into the Pneumococcal Chromosome

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