Full-length rat amylin forms fibrils following substitution of single residues from human amylin. [electronic resource]
- Journal of molecular biology Feb 2003
- 1147-56 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0022-2836
10.1016/s0022-2836(02)01377-3 doi
Amino Acid Sequence Amyloid--chemistry Animals Humans Islet Amyloid Polypeptide Microscopy, Atomic Force Molecular Sequence Data Peptides--chemistry Proline--metabolism Protein Conformation Rats Sequence Alignment Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization