Document Detail


A Partially Folded State of Ovalbumin at Low pH Tends to Aggregate.
MedLine Citation:
PMID:  20703954     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
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.
Authors:
Aabgeena Naeem; Taqi Ahmed Khan; Mohammad Muzaffar; Saman Ahmad; M Saleemuddin
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Cell biochemistry and biophysics     Volume:  59     ISSN:  1559-0283     ISO Abbreviation:  Cell Biochem. Biophys.     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2010-12-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9701934     Medline TA:  Cell Biochem Biophys     Country:  United States    
Other Details:
Languages:  eng     Pagination:  29-38     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Faculty of Life Science, AMU, Aligarh, 202 002, India, aabgeenanaim@rediffmail.com.
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