Dinard Herbarium: A Source of Information to Infer Temporal Changes in Seaweed Communities?

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Typification of the Mediterranean endemic deep-water macroalga <I>Laminaria rodriguezii</I> Bornet (Laminariaceae, Phaeophyceae)

La lectotypification de l’algue brune endémique de la mer Méditerranée, Laminaria rodriguezii Bornet (Laminariaceae), est basée sur le protologue et le matériel original de Bornet conservé à l’Herbier de Cryptogamie du Muséum National d’Histoire Naturelle de Paris (PC).Laminaria rodriguezii Bornet is a deep-water brown alga endemic of the Mediterranean Sea. Lectotypification of Laminaria rodiguezii has been based on both Bornet’s protologue and the original material housed at the cryptogamic collections of the Muséum National d’Histoire Naturelle de Paris (PC).</p

In Honor of Denis Lamy

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A New Species of Stenogramma was Uncovered Indian Ocean during the Expedition Atimo Vatae: Stenogramma lamyi sp. nov.

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New chaetoglobosins from maize infested by Phomopsis leptostromiformis fungi. Production, identification, and semi‒synthesis

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Herbier de Dinard : Histoire du laboratoire maritime

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Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization

International audienceUltraviolet (UV) synchrotron radiation circular dichroism (SRCD) spectroscopy has made an important contribution to the determination and understanding of the structure of bio-molecules. In this paper, we report an innovative approach that we term time-resolved SRCD (tr-SRCD), which overcomes the limitations of current broadband UV SRCD setups. This technique allows accessing ultrafast time scales (down to nanoseconds), previously measurable only by other methods, such as infrared (IR), nuclear magnetic resonance (NMR), fluorescence and absorbance spectroscopies and small angle X-ray scattering (SAXS). The tr-SRCD setup takes advantage of the natural polarisation of the synchrotron radiation emitted by a bending magnet to record broadband UV CD faster than any current SRCD setup, improving the acquisition speed from 10 mHz to 130 Hz and the accessible temporal resolution by several orders of magnitude. We illustrate the new approach by following the isomers concentration changes of an azopeptide after a photoisomerisation. This breakthrough in SRCD spectroscopy opens up a wide range of potential applications to the detailed characterisation of biological processes, such as protein folding, protein-ligand binding