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The hydrophilic loop region of the CF0 c subunit has been expressed as a fusion with MalE in Escherichia coli. A cysteine was introduced at the C-terminus to allow fluorophore labeling of the fusion protein. After removal of the MalE moiety, the labeled peptide was used for binding studies with fluorophore-labeled CF1. At saturation, 1 mol peptide was bound per mol CF1. Binding was abolished after removal of subunit epsilon from CF1, and partially restored by addition of recombinant epsilon.
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Licher et al. (1998) studied this question.
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