Evaluation of Copper2+ Affinities for the Prion Protein
Author:
Affiliation:
1. School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, U.K.
2. Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, U.K.
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi9011397
Reference35 articles.
1. Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible
2. Dynamics of a truncated prion protein, PrP(113-231), from15N NMR relaxation: Order parameters calculated and slow conformational fluctuations localized to a distinct region
3. Deconvoluting the Cu2+ Binding Modes of Full-length Prion Protein
4. The cellular prion protein binds copper in vivo
5. Probing Copper2+ Binding to the Prion Protein Using Diamagnetic Nickel2+ and 1H NMR: The Unstructured N terminus Facilitates the Coordination of Six Copper2+ Ions at Physiological Concentrations
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