NR AIIS
AU Mihara,H.; Takahashi,Y.
TI Engineering peptides and proteins that undergo alpha-to-beta transitions
QU Current Opinion in Structural Biology 1997 Aug; 7(4): 501-8
ER Curr Opin Struct Biol 1997 Oct;7(5):749
PT journal article; review; review, tutorial
AB 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.
ZR 56
MH Amino Acid Sequence; Animal; Human; Mice; Molecular Sequence Data; Protein Conformation; Protein Engineering/methods; *Protein Folding; Proteins/*chemistry
AD Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo, Institute of Technology, Yokohama, Japan. hmihara@bio.titech.ac.jp
SP englisch
PO England