https://www.selleckchem.com/products/pf-8380.html
6 ± 0.3 kcal/mol and ΔS⧧= -4.9 ± 0.8 cal/(mol K).The dynamics of peptide-protein binding and unbinding of a variant of the RNase S system has been investigated. To initiate the process, a photoswitchable azobenzene moiety has been covalently linked to the S-peptide, thereby switching its binding affinity to the S-protein. Transient fluorescence quenching was measured with the help of a time-resolved fluorometer, which has been specifically designed for these experiments and is based on inexpensive light-emitting diodes and laser diodes
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