NR AEYZ
AU Gustiananda,M.; Haris,P.I.; Milburn,P.J.; Gready,J.E.
TI Copper-induced conformational change in a marsupial prion protein repeat peptide probed using FTIR spectroscopy
QU FEBS Letters 2002 Feb 13; 512(1-3): 38-42
PT journal article
AB We report the first Fourier transform infrared analysis of prion protein (PrP) repeats and the first study of PrP repeats of marsupial origin. Large changes in the secondary structure and an increase in hydrogen bonding within the peptide groups were evident from a red shift of the amide I band by >7 cm(-1) and an approximately five-fold reduction in amide hydrogen-deuterium exchange for peptide interacting with Cu(2+) ions. Changes in the tertiary structure upon copper binding were also evident from the appearance of a new band at 1564 cm(-1), which arises from the ring vibration of histidine. The copper-induced conformational change is pH dependent, and occurs at pH >7.
MH Animal; Copper/pharmacology; Opossums/*physiology; Prions/*chemistry/metabolism; Protein Structure, Secondary/drug effects; Protein Structure, Tertiary/drug effects; Repetitive Sequences, Amino Acid; Spectroscopy, Fourier Transform Infrared; Support, Non-U.S. Gov't
AD Computational Molecular Biology and Drug Design Group, John Curtin School of Medical Research, Australian National University, Canberra.
SP englisch
PO Niederlande