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lupinus albicaulis/çürük

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NesneKlinik denemelerPatentler
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Lupinus luteus pathogenesis-related protein as a reservoir for cytokinin.

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Plant pathogenesis-related (PR) proteins of class 10 (PR-10) are small and cytosolic. The main feature of their three-dimensional structure is a large cavity between a seven-stranded antiparallel beta-sheet and a long C-terminal alpha-helix. Although PR-10 proteins are abundant in plants, their

Cytokinin-induced structural adaptability of a Lupinus luteus PR-10 protein.

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Plant pathogenesis-related (PR) proteins of class 10 are the only group among the 17 PR protein families that are intracellular and cytosolic. Sequence conservation and the wide distribution of PR-10 proteins throughout the plant kingdom are an indication of an indispensable function in plants, but
LlPR-10.2B, a Pathogenesis-related class 10 (PR-10) protein from yellow lupine (Lupinus luteus) was crystallized in complex with melatonin, an emerging important plant regulator and antioxidant. The structure reveals two molecules of melatonin bound in the internal cavity of the protein, plus a very
The objective was to test the effects of replacing soybean meal in dairy cow diets with either raw or extruded faba bean:linseed or lupin:linseed blends on intake, milk yield and composition, N partitioning, and ruminal and plasma parameters. Our main hypotheses were that N from extruded blends was

Structure of a yellow lupin pathogenesis-related PR-10 protein belonging to a novel subclass.

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Pathogenesis-related (PR) proteins of class 10 are abundant in higher plants. Some of these proteins are induced under stress conditions as part of the plant defence mechanism. Other homologues are developmentally regulated and their expression varies in different plant organs. The PR-10 proteins

Crystallographic and CD probing of ligand-induced conformational changes in a plant PR-10 protein.

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Plant pathogenesis-related class 10 (PR-10) proteins are a family of abundant proteins initially identified as elements of the plant defense system. The key structural feature suggesting PR-10 functionality is a huge hydrophobic cavity created in the protein interior by a scaffold composed of an
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