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https://www.selleckchem.com/products/Y-27632.html Combined neutron and X-ray powder diffraction techniques highlighted the sorption capacity of the acidic L zeolite towards the L-lysine amino acid. The role of zeolite channels in the stabilization of the lysine absorbed and the effect of water on protein structure are elucidated at atomistic level. The stabilization of the L α-helical conformation is related to strong H-bonds between the tail aminogroups of lysine molecules and the Brønsted acid site as well as to complex intermolecular H-bond system between water molecules, zeolite and amino acid. This finding is relevant in the catalytic synthesis of polypeptide, as well as in industrial biotechnology by qualitatively predicting binding behaviour.Invited for this month's cover are the groups of Annalisa Martucci and Luisa Pasti at the University of Ferrara (Italy). The cover picture shows L-lysine amino acid adsorption on zeolite L. The role of zeolite channels in the stabilization of the lysine absorbed and the effect of water on protein structure are elucidated at atomistic level. The stabilization of the L α-helical conformation is related to strong H-bonds between the tail aminogroups of lysine molecules and the Brønsted acid site as well as to complex intermolecular H-bond system between water molecules, zeolite and amino acid. Read the full text of their Full Paper at 10.1002/open.202000183.Chlorophyll fluorescence (ChlF) has been used to understand photosynthesis and its response to climate change, particularly with satellite-based data. However, it remains unclear how the ChlF ratio and photosynthesis are linked at the leaf level under drought stress. Here, we examined the link between ChlF ratio and photosynthesis at the leaf level by measuring photosynthetic traits, such as net CO2 assimilation rate (An), the maximum carboxylation rate of Rubisco (Vcmax), the maximum rate of electron transport (Jmax), stomatal conductance (gs) and total chlorophyll conte

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