Comparative Analysis of the Human and Chicken Prion Protein Copper Binding Regions at pH 6.5*□S
نویسندگان
چکیده
From the ‡Center of Experimental Medicine, Institute of Biochemistry and Molecular Biology I, University Hospital Hamburg-Eppendorf, c/o Deutsches Elektronen Synchrotron (DESY), and the §European Molecular Biology Laboratory, Outstation Hamburg at DESY, 22603 Hamburg, Germany, the ¶Bernhard-Nocht-Institute for Tropical Medicine, 20359 Hamburg, Germany, the Institute of Organic Chemistry, Bulgarian Academy of Sciences, Sofia 1113, Bulgaria, the **Institute of Physiological Chemistry, University of Tübingen, 72076 Tübingen, Germany, and the ‡‡Institute of Biochemistry and Food Chemistry, University of Hamburg, 20146 Hamburg, Germany
منابع مشابه
Chicken prion tandem repeats form a stable, protease-resistant domain.
Prion-linked diseases, such as mad cow disease, scrapie, and the human genetic disorder Creutzfeldt-Jakob disease, are fatal neurodegenerative diseases correlated with changes in the secondary structure of neural prion protein. We expressed recombinant chicken prion protein in Escherichia coli and purified the protein to homogeneity. Circular dichroism spectra of the 26 kDa recombinant protein ...
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Combined potentiometric, calorimetric and spectroscopic methods were used to investigate the Cu(2+) binding ability and coordination behaviour of some peptide fragments related to the neurotoxic region of chicken Prion Protein. The systems studied were the following protein fragments: chPrP(106-114), chPrP(119-126), chPrP(108-127), chPrP(105-127) and chPrP(105-133).The complex formation always ...
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