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- Title
Empirical rules for rationalising visible circular dichroism of Cu<sup>2+</sup> and Ni<sup>2+</sup> histidine complexes: Applications to the prion protein
- Authors
Klewpatinond, Mark; Viles, John H.
- Abstract
Abstract: A natively unfolded region of the prion protein, PrP(90–126) binds Cu2+ ions and is vital for prion propagation. Pentapeptides, acyl-GGGTH92–96 and acyl-TNMKH107–111, represent the minimum motif for this Cu2+ binding region. EPR and 1H 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 His96 and His111 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 Cu2+ visible CD spectra involving histidine and amide main-chain coordination.
- Subjects
NUCLEAR magnetic resonance; SPECTRUM analysis; ATOMS; BIOCHEMISTRY
- Publication
FEBS Letters, 2007, Vol 581, Issue 7, p1430
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2007.02.068