Document Detail

Reversible aggregation of mouse prion protein derivatives with PrPSC-like structural properties.
MedLine Citation:
PMID:  12760416     Owner:  NLM     Status:  MEDLINE    
Three carbamylated derivatives of reduced mouse prion protein (mPrP) were isolated during the aborted oxidative folding in the presence of urea. These three prion protein derivatives (mPrP-a, mPrP-b, and mPrP-c) exist as monomer in the acidic solution (pH < 2.0) and exhibit prevalent random coil structure. However, they undergo rapid aggregation and transformation to a predominant beta-sheet structure upon exposure to ionic buffer with pH greater than 3.0. The stability of aggregates of mPrP conformers is in part dependent upon the time that they were allowed to develop. The nascent aggregates comprise a significant fraction of loosely packed mPrP monomers that can be dissociated by treatment with strong acidic solution. Matured aggregates acquired through prolonged sample incubation contain more tightly packed mPrP monomers that cannot be dissociated by strong acid but can be disaggregated by denaturant. The properties of reversible aggregation of mPrP-a, mPrP-b, and mPrP-c bear a striking resemblance to that observed with aggregates of hamster PrPSC.
Bao-Yuan Lu; Ivo Atanasov; Z Hong Zhou; Jui-Yoa Chang
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of protein chemistry     Volume:  22     ISSN:  0277-8033     ISO Abbreviation:  J. Protein Chem.     Publication Date:  2003 Feb 
Date Detail:
Created Date:  2003-05-22     Completed Date:  2004-02-03     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8217321     Medline TA:  J Protein Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  115-26     Citation Subset:  IM    
Research Center for Protein Chemistry, Institute of Molecular Medicine, Department of Biochemistry and Molecular Biology, The University of Texas, Houston, Texas 77030, USA.
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MeSH Terms
Circular Dichroism
Hydrogen-Ion Concentration
Microscopy, Electron
Molecular Weight
PrPSc Proteins / chemistry*,  isolation & purification
Prions / chemistry*,  isolation & purification
Protein Denaturation
Protein Folding*
Protein Structure, Secondary
Urea / chemistry
Grant Support
Reg. No./Substance:
0/Buffers; 0/PrPSc Proteins; 0/Prions; 57-13-6/Urea

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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