NR ACLR
AU Chae,Y.K.; Cho,K.S.; Chun,W.
TI A prionogenic peptide derived from Sup35 can force the whole GST fusion protein to show amyloid characteristics
QU Protein and Peptide Letters 2002 Aug; 9(4): 315-21
PT journal article
AB A prion determining 7-mer peptide derived from Sup35 was fused to glutathione S transferase (GST). The fusion protein was successfully overexpressed in Escherichia coli, and purified by employing affinity chromatography. Upon incubation, it showed substantial aggregation suggesting the formation of amyloid-like fibrils. Congo Red binding strongly suggested that the fusion protein formed amyloid-like fibrils. By considering the steric hindrance of GST, the beta-sheet formation should be in the anti-parallel fashion.
MH Congo Red/metabolism; Dyes/metabolism; Escherichia coli/genetics/metabolism; Fungal Proteins/genetics/*metabolism; Genes, Reporter; Peptides/genetics/*metabolism; Prions/*metabolism; Protein Structure, Secondary; Recombinant Fusion Proteins/genetics/*metabolism; Support, Non-U.S. Gov't
AD Department of Applied Chemistry and Recombinant Protein Expression Center (RPEC), Sejong University, 98 Gunja-Dong, Gwangjin-Gu, Seoul, 143-747, Korea.
SP englisch
PO Niederlande