Thread: NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
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Default NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.

NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.

Chem Commun (Camb). 2011 Jun 14;47(22):6407-9

Authors: Shoshan MS, Shalev DE, Adriaens W, Merkx M, Hackeng TM, Tshuva EY

Abstract
The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ~3.0 and ~6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH ~8.5. This suggests a possible role of Met in metal transport.


PMID: 21552638 [PubMed - indexed for MEDLINE]



Source: PubMed
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