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Competing intrachain interactions regulate the formation of beta-sheet fibrils in bovine PrP peptides.

Abstract:

At the heart of the pathogenesis of transmissible spongiform encephalopathies (TSEs), such as BSE, scrapie, and Creutzfeldt-Jakob disease, lies a poorly understood structural rearrangement of PrP, an abundant glycoprotein of the nervous and lymphoid systems. The normal form (PrP(C)), rich in alpha-helix, converts into an aberrant beta-sheet-dominated form (PrP(Sc)), which seems to be at the center of the pathotoxic symptoms observed in TSEs. To understand this process better at a molecular le...

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Publication status:
Published

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Publisher copy:
10.1110/ps.0236703
Journal:
Protein science : a publication of the Protein Society More from this journal
Volume:
12
Issue:
3
Pages:
600-608
Publication date:
2003-03-01
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
Language:
English
Keywords:
Pubs id:
pubs:14064
UUID:
uuid:ad98d2fb-c799-44ea-ba56-d622cb96649d
Local pid:
pubs:14064
Source identifiers:
14064
Deposit date:
2012-12-19

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