- Abstract:
-
The substitution of alanines for the two cysteines which form thioether linkages to the haem group in cytochrome c(552) from Hydogenobacter thermophilus destabilises the native protein fold. The holo form of this variant slowly converts into a partially folded apo state that over prolonged periods of time aggregates into fibrillar structures. Characterisation of these structures by electron microscopy and thioflavin-T binding assays shows that they are amyloid fibrils. The data demonstrate th...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/s0014-5793(01)02384-5
-
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- Journal:
- FEBS letters
- Volume:
- 495
- Issue:
- 3
- Pages:
- 184-186
- Publication date:
- 2001-04-05
- DOI:
- EISSN:
-
1873-3468
- ISSN:
-
0014-5793
- URN:
-
uuid:e05ff94f-96f2-4b27-b3f8-3211529019ee
- Source identifiers:
-
31868
- Local pid:
- pubs:31868
- Language:
- English
- Keywords:
- Copyright date:
- 2001
Journal article
Amyloid fibril formation by a helical cytochrome.
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