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Important Contributions of a New Quantitative Preparative Native Continuous Polyacrylamide Gel Electrophoresis (QPNC-PAGE) Procedure for Elucidating Metal Cofactor Metabolisms in Protein-Misfolding Diseases - A Theory

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The quantitative analysis of metallochaperone proteins in biofluids (e.g. blood, liquor) may be a major prerequisite for clinical investigations concerning the structure-function relationships of biologically-active metal cofactorcontaining chaperones in protein-misfolding diseases (e.g. Alzheimer's or related diseases). For these purposes, a new state-of-the-art gel electrophoresis [quantitative preparative native continuous polyacrylamide gel electrophoresis procedure (QPNC-PAGE)] combined with biological mass and NMR spectrometries might essentially contribute to provide fundamental insights into the metabolisms of important metal cofactors in biological systems and the proper folding of metallochaperones in conformational diseases.

Keywords: Alzheimer's disease; Biologically-active metallochaperones; Chemical stability; GPC; ICP-MS; Metal cofactorcontaining proteins; NMR; Native conformation; QPNC-PAGE; Quantitative analysis

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606776819637

Affiliations: Institute for Chemistry and Dynamics of the Geosphere, Institute III: Phytosphere, Research Centre Juelich, Juelich 52425, Germany.

Publication date: May 1, 2006

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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