- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/s0006-3495(00)76560-x
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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
- Copyright date:
- 2000
Journal article
Ultrastructural organization of amyloid fibrils by atomic force microscopy.
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