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Copper‐induced conformational change in a marsupial prion protein repeat peptide probed using FTIR spectroscopy
Author(s) -
Gustiananda Marsia,
Haris Parvez I.,
Milburn Peter J.,
Gready Jill E.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03298-7
Subject(s) - peptide , copper , amide , chemistry , fourier transform infrared spectroscopy , crystallography , protein secondary structure , histidine , hydrogen–deuterium exchange , conformational change , marsupial , infrared spectroscopy , hydrogen bond , protein structure , spectroscopy , biophysics , hydrogen , amino acid , stereochemistry , molecule , biochemistry , biology , organic chemistry , physics , quantum mechanics , paleontology
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.