Pinning down flavoproteins: A designed β-hairpin peptide binds flavin mononucleotide (FMN) in water through noncovalent interactions involving Trp and Lys residues on one face of the β hairpin (see model). Reduction of FMN is disfavored in the complex as a result of favorable π–π stacking interactions between Trp side chains and the oxidized flavin ring. This system mimicks the function of naturally occurring flavoproteins.
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Butterfield et al. (2004) studied this question.
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