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The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner.

Abstract:

Amyloid fibrils are typically rigid, unbranched structures with diameters of approximately 10 nm and lengths up to several micrometres, and are associated with more than 20 diseases including Alzheimer's disease and type II diabetes. Insulin is a small, predominantly alpha-helical protein consisting of 51 residues in two disulfide-linked polypeptide chains that readily assembles into amyloid fibrils under conditions of low pH and elevated temperature. We demonstrate here that both the A-chain...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2006.05.007

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Journal:
Journal of molecular biology
Volume:
360
Issue:
2
Pages:
497-509
Publication date:
2006-07-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:2be94c37-1ccd-466e-9fb1-2cc32d17b73a
Source identifiers:
59290
Local pid:
pubs:59290

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