The alpha-pleated sheet, a secondary structure proposed by Pauling and Corey, is rarely found in proteins. It has a residue length of 3Å compared to 3.3Å for the more common beta-sheet conformation found in many proteins.
The modelisation of conformational changes of amyloid proteins (under the low pH conditions that favor amyloid fibril formation) has suggested that the acquisition of an alpha-pleated sheet oligomeric intermediate could be the target of an antibody that blocks toxicity.
|||Armen, R.S. et al., Proc. Natl. Acad. Sci. USA, 101, 11622-11627 (2004). PMID: 15280548|