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  • Title: A partially folded state of ovalbumin at low pH tends to aggregate.
    Author: Naeem A, Khan TA, Muzaffar M, Ahmad S, Saleemuddin M.
    Journal: Cell Biochem Biophys; 2011 Jan; 59(1):29-38. PubMed ID: 20703954.
    Abstract:
    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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