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Amyloid fibril formation by a helical cytochrome.

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...

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Publication status:
Published

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Authors


Pertinhez, TA More by this author
Bouchard, M More by this author
Tomlinson, EJ More by this author
Ferguson, SJ More by this author
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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

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