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Spectroscopic and Functional Characterization of Human β-Synuclein

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To elucidate potential biological roles of human β-synuclein, we studied its conformational changes under various conditions. The structural and functional properties of β-synuclein were characterized using biochemical and biophysical methods including: a functional assay, mass spectrometry, size exclusion chromatography, circular dichroism (CD), and fluorescence spectroscopy. The results showed β-synuclein has a high proportion of random coil in solution.

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Keywords: circular dichroism; conformational change; fluorescence; β-Synuclein

Document Type: Research Article

Publication date: 01 October 2007

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  • 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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