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https://www.selleckchem.com/products/mycro-3.html N concentrations of shoots were the most efficient for evaluating genotypic tolerance. Low nitrate reductase (NR) and glutamine synthetase (GS) activity might be key factors limiting N accumulation. Chlorophyll (Chl) content and net photosynthetic rate, as well as stomatal conductance and evaporation, were useful for identifying salinity tolerance physiological mechanisms, but the effectiveness was low for genotypic tolerance testing for forage type oats due to the interaction between genotypes and salinity levels. The selection of high salinity-tolerant genotypes should focus on genotypes with photosynthetic resilience to salt, followed by high N metabolism (higher NR and GS activities) to ensure accumulation of more N in the shoot dry matter.The natively unfolded nature of intrinsically disordered proteins (IDPs) relies on several physicochemical principles, of which the balance between a low sequence hydrophobicity and a high net charge appears to be critical. Under this premise, it is well-known that disordered proteins populate a defined region of the charge-hydropathy (C-H) space and that a linear boundary condition is sufficient to distinguish between folded and disordered proteins, an approach widely applied for the prediction of protein disorder. Nevertheless, it is evident that the C-H relation of a protein is not unalterable but can be modulated by factors extrinsic to its sequence. Here, we applied a C-H-based analysis to develop a computational approach that evaluates sequence disorder as a function of pH, assuming that both protein net charge and hydrophobicity are dependent on pH solution. On that basis, we developed DispHred, the first pH-dependent predictor of protein disorder. Despite its simplicity, DispHred displays very high accuracy in identifying pH-induced order/disorder protein transitions. DispHred might be useful for diverse applications, from the analysis of conditionally disordered segmen

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