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Ultrastructural organization of amyloid fibrils by atomic force microscopy.

Abstract:

Atomic force microscopy has been employed to investigate the structural organization of amyloid fibrils produced in vitro from three very different polypeptide sequences. The systems investigated are a 10-residue peptide derived from the sequence of transthyretin, the 90-residue SH3 domain of bovine phosphatidylinositol-3'-kinase, and human wild-type lysozyme, a 130-residue protein containing four disulfide bridges. The results demonstrate distinct similarities between the structures formed b...

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Publication status:
Published

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Journal:
Biophysical journal
Volume:
79
Issue:
6
Pages:
3282-3293
Publication date:
2000-12-05
DOI:
EISSN:
1542-0086
ISSN:
0006-3495
URN:
uuid:ca544694-e4fe-4120-86fc-0f2046e8d95f
Source identifiers:
31790
Local pid:
pubs:31790

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