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Abstract
Reversible photocontrol of peptide and protein conformation could prove to be a powerful
tool for probing function in diverse biological systems. Here, we report reversible
photoswitching of the helix content in short peptides containing an azobenzene cross-linker
between cysteine residues at positions i, i + 4, or i, i + 11 in the sequence. Trans-to-cis
photoisomerization significantly increases the helix content in the i, i + 4 case
and significantly decreases the helix content in the i, i + 11 case. These cross-linker
designs significantly expand the possibilities for photocontrol of peptide and protein
structure.