Publication: Photocontrolling Protein–Peptide Interactions: From Minimal Perturbation to Complete Unbinding
Photocontrolling Protein–Peptide Interactions: From Minimal Perturbation to Complete Unbinding
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Jankovic, B., Gulzar, A., Zanobini, C., Bozovic, O., Wolf, S., Stock, G., & Hamm, P. (2019). Photocontrolling Protein–Peptide Interactions: From Minimal Perturbation to Complete Unbinding. Journal of the American Chemical Society, 141, 10702–10710. https://doi.org/10.1021/jacs.9b03222
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Abstract
An azobenzene-derived photoswitch has been covalently cross-linked to two sites of the S-peptide in the RNase S complex in a manner that the alpha-helical content of the S-peptide reduces upon cis-to-trans isomerization of the photoswitch. Three complementary experimental techniques have been employed, isothermal titration calorimetry, circular dichroism spectroscopy and intrinsic tyrosine fluorescence quenching, to determine the binding affinity of the S-peptide to the S-protein in the two states of the photoswitch. Five mutants with
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Jankovic, B., Gulzar, A., Zanobini, C., Bozovic, O., Wolf, S., Stock, G., & Hamm, P. (2019). Photocontrolling Protein–Peptide Interactions: From Minimal Perturbation to Complete Unbinding. Journal of the American Chemical Society, 141, 10702–10710. https://doi.org/10.1021/jacs.9b03222