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The protofilament structure of insulin amyloid fibrils.

Abstract:

Under solution conditions where the native state is destabilized, the largely helical polypeptide hormone insulin readily aggregates to form amyloid fibrils with a characteristic cross-beta structure. However, there is a lack of information relating the 4.8 A beta-strand repeat to the higher order assembly of amyloid fibrils. We have used cryo-electron microscopy (EM), combining single particle analysis and helical reconstruction, to characterize these fibrils and to study the three-dimension...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.142459399

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Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
99
Issue:
14
Pages:
9196-9201
Publication date:
2002-07-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:f424bdc3-fcbc-4177-8089-0ae28e7759a1
Source identifiers:
59371
Local pid:
pubs:59371

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