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  • Title: The distance separating Cys-10 from the high-affinity metal binding site in actin.
    Author: Miki M, Barden JA, dos Remedios CG.
    Journal: Biochem Int; 1986 Jun; 12(6):807-13. PubMed ID: 3741444.
    Abstract:
    The fluorescence resonance energy transfer between 5-[2-[iodoacetyl)amino)ethyl]aminonaphthalene-1-sulphonic acid (1,5-IAEDANS) attached to Cys-10 residue and Co2+ bound to the high affinity metal site was measured. The resonance energy transfer efficiency was 8 +/- 2%, which corresponds to a distance of 2.1 nm using the absorption spectrum of Co-EDTA and 3.0 nm using the more relevant absorption spectrum of Co2+ bound to carboxypeptidase as a model spectrum of Co2+ bound to actin, respectively.
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