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Selenomethionine, p -cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure

Abstract

The use of selenomethionine (MSe)-p-cyanophenylalanine (FCN) pairs to probe protein structure is demonstrated. MSe quenches FCN fluorescence via electron transfer. Both residues can be incorporated recombinantly or by peptide synthesis. Time-resolved and steady-state fluorescence measurements demonstrate that MSe-FCN pairs provide specific local probes of helical structure.

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