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Empirical rules for rationalising visible circular dichroism of Cu 2+ and Ni 2+ histidine complexes: Applications to the prion protein
Author(s) -
Klewpatid Mark,
Viles John H.
Publication year - 2007
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/j.febslet.2007.02.068
Subject(s) - histidine , chemistry , crystallography , amide , circular dichroism , spectral line , electron paramagnetic resonance , peptide , stereochemistry , ion , amino acid , nuclear magnetic resonance , biochemistry , organic chemistry , physics , astronomy
A natively unfolded region of the prion protein, PrP(90–126) binds Cu 2+ ions and is vital for prion propagation. Pentapeptides, acyl‐GGGTH 92–96 and acyl‐TNMKH 107–111 , represent the minimum motif for this Cu 2+ binding region. EPR and 1 H NMR suggests that the coordination geometry for the two binding sites is very similar. However, the visible CD spectra of the two sites are very different, producing almost mirror image spectra. We have used a series of analogues of the pentapeptides containing His 96 and His 111 to rationalise these differences in the visible CD spectra. Using simple histidine‐containing tri‐peptides we have formulated a set of empirical rules that can predict the appearance of Cu 2+ visible CD spectra involving histidine and amide main‐chain coordination.