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Structural Changes and Aggregation Process of Cu/Containing Amine Oxidase in the Presence of 2,2,2'-Trifluoroethanol

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Conformational and structural changes of lentil seedlings amine oxidase (LSAO) were studied in the presence of trifluoroethanol (TFE) by spectroscopic and analytical techniques. At TFE concentrations up to 5%, the induction of a structural transition from β-sheet to α-helix and up to 10% TFE a structural transition from α-helix to β-sheet as well as inactivation of the enzyme are observed. At TFE concentrations between 10-35%, LSAO proves to be prone to aggregation and beyond 35% TFE leads to a non-native protein structure with a high α-helix content. The obtained results revealed that the aggregation of LSAO is strongly linked to the nature of secondary structures.

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Keywords: Aggregation; Amine oxidase; Circular dichroism; Fluorescence; Secondary structure; TFE

Document Type: Research Article

Publication date: June 1, 2008

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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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