Engineering peptides and proteins that undergo alpha-to-beta transitions.
In the 'protein-only' hypothesis, prion diseases are proposed to be the result of conformational changes of the normal form of the prion protein (PrPC) with a highly alpha-helical conformation to a pathogenic scrapie form (PrPSc) with a predominantly beta-sheet conformation. Recent studies examining the folding process of proteins, as well as the amyloidogenesis of peptides and proteins including prion proteins, Alzheimer's beta-peptides and other pathogenic protein mutants, have provided insight into the conformational changes essential to fibrillogenesis and correct folding.
Mihara
H
H
Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo, Institute of Technology, Yokohama, Japan. hmihara@bio.titech.ac.jp
Takahashi
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D011506:Proteins