Journal
CHEMISTRY & BIOLOGY
Volume 9, Issue 3, Pages 391-397Publisher
CELL PRESS
DOI: 10.1016/S1074-5521(02)00109-6
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Reversible photocontrol of peptide and protein conformation could prove to be a powerful too[ 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.
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