| A Partially Folded State of Ovalbumin at Low pH Tends to Aggregate. | |
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MedLine Citation:
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PMID: 20703954 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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At pH 2, ovalbumin retains native-like secondary structure as seen by far-UV CD and FTIR, but lacks well-defined tertiary structure as seen by the fluorescence and near-UV CD spectra. Addition of 20 mM Trifluoroacetic acid (TFA) or 30 mM Trichloroacetic acid (TCA) on acid-induced state results in protein aggregation. This aggregated state possesses extensive β-sheet structure as revealed by far-UV CD and FTIR spectroscopy. Furthermore, the aggregates exhibit decreased ANS fluorescence and increased thioflavin T fluorescence. The presence of aggregates was confirmed by size exclusion chromatography. Such a formation of β-sheet structure is found in the amyloid of a number of neurological diseases such as Alzheimer's and scrapie. Ovalbumin at low pH, in the presence of K(2)SO(4), exists in partially folded state characterized by native-like secondary structure and tertiary folds. |
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Authors:
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Aabgeena Naeem; Taqi Ahmed Khan; Mohammad Muzaffar; Saman Ahmad; M Saleemuddin |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Cell biochemistry and biophysics Volume: 59 ISSN: 1559-0283 ISO Abbreviation: Cell Biochem. Biophys. Publication Date: 2011 Jan |
Date Detail:
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Created Date: 2010-12-21 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9701934 Medline TA: Cell Biochem Biophys Country: United States |
Other Details:
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Languages: eng Pagination: 29-38 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Faculty of Life Science, AMU, Aligarh, 202 002, India, aabgeenanaim@rediffmail.com. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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