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Titlebook: Interacting Protein Domains; Their Role in Signal Ludwig Heilmeyer Conference proceedings 1997 Springer-Verlag Berlin Heidelberg 1997 ATP.A

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Interaction of Protein Kinase A, from , with Proteins and Peptides: Comparison with the Mammalian Enile they are highly specific for ATP as phosphate donor (only a small minority uses GTP as an alternative), their limited . specificity for protein substrates is remarkable with regard to the specialized functions of protein kinases in signal transduction, and cellular and metabolic regulation. Most
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Interaction Studies Using Biosensorsr the characterization of protein-protein, protein-DNA and ligand-receptor interactions (for review see Szabo, ., 1995; Raghavan .., 1995) by measuring directly the binding of an analyte to a ligand immobilized on a sensor surface. The chemistries for coupling molecules to the surface via amine, sul
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Advances in Determination of Protein Structure by X-ray Diffraction Methodsis essential for understanding the biological function of macromolecules. In the early days, protein crystallography was laborious and uncertain. The situation is different today. In the last decade the technique has seen many spectacular technical advances that allows a new structure to be determin
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Binding studies with SH2 domains from the phosphotyrosine kinase ZAP70 using surface plasmon resonanly much interest in the identification and characterisation of these proteins, in the expectation that alteration of these interactions mght lead to modulation of the immune response. A model of some of the proteins in the activated TCR complex is shown in Figure 1.
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Proteins at Work: Time-Resolved FTIR Studies of Bacteriorhodopsin and the GTP-Binding Protein P21nisms of proteins at the atomic level.. Complementary to NMR spectroscopy and x-ray structure analysis, which provide the static protein ground state structure with atomic resolution, time-resolved FT-IR difference spectroscopy monitors the dynamics of proteins at the atomic level. Although infrared
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Regulation of Phospholipase C isozymesfined and named by the position they attack on the phospholipid backbone. Phospholipase A. (PLA.) catalyzes the hydrolysis of the fatty acid group on the middle (sn-2) position while phospholipase C (PLC) catalyzes the hydrolysis of the phosphodiester bond on the third (sn-3) position of the glycero
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