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The English familial mutation of beta-amyloid peptide dramatically increases risk of Alzheimer's disease. The peptide carrying this mutation is much more prone to pathological zinc-induced dimerization than a normal beta-amyloid, and the formed dimeric complexes might be toxic for neural system. The mechanism of dimerization was studied using various NMR techniques. The set of amino acid residues involved into the zinc binding, the stoichiometry, and the parameters describing exchange between monomeric and dimeric forms of the zinc-peptide complex were determined. High resolution spatial structure of the dimeric complex was determined based on NMR data.