Ultrastructural organization of amyloid fibrils by atomic force microscopy.

@article{Chamberlain2000UltrastructuralOO,
  title={Ultrastructural organization of amyloid fibrils by atomic force microscopy.},
  author={Aaron K. Chamberlain and Cait E. MacPhee and Jes{\'u}s Zurdo and Ludmilla A Morozova-Roche and H. Allen O. Hill and Christopher M. Dobson and Jason J Davis},
  journal={Biophysical journal},
  year={2000},
  volume={79 6},
  pages={3282-93}
}
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… CONTINUE READING