- 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...
Expand abstract - Publication status:
- Published
- 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
- Copyright date:
- 2002
Journal article
The protofilament structure of insulin amyloid fibrils.
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