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https://www.selleckchem.com/products/elacridar-gf120918.html To spatially control biochemical functions at specific sites within a genome, we have engineered a synthetic switch that activates when bound to its DNA target site. The system uses two CRISPR-Cas complexes to colocalize components of a de novo-designed protein switch (Co-LOCKR) to adjacent sites in the genome. Colocalization triggers a conformational change in the switch from an inactive closed state to an active open state with an exposed functional peptide. We prototype the system in yeast and demonstrate that DNA binding triggers activation of the switch, recruitment of a transcription factor, and expression of a downstream reporter gene. This DNA-triggered Co-LOCKR switch provides a platform to engineer sophisticated functions that should only be executed at a specific target site within the genome, with potential applications in a wide range of synthetic systems including epigenetic regulation, imaging, and genetic logic circuits.This study investigated the interaction between N-acetyl-l-cysteine (NAC) and ovalbumin (OVA) using multispectroscopic technology, molecular docking, and quartz crystal microbalance with dissipation (QCM-D). Fluorescence intensity and UV absorption of OVA were decreased substantially upon the addition of NAC. The calculated Kq values were obtained at 298, 304, and 310 K for 13.48, 15.59, and 17.50 (× 1012 L mol-1), respectively, suggesting that the static quenching was dominated. Thermodynamic parameters such as ΔH (-150.58 kJ mol-1), ΔS (-433.51 J mol-1 K-1), and ΔG values (-21.39 kJ mol-1), combined with molecular docking and QCM-D data, showed that the interaction was spontaneous and van der Waals and hydrogen bonding were identified as the main driving forces. FTIR and CD results showed that the α-helix content of OVA increased from 2.8 to 22.9%, and the β-sheet decreased from 0.2 to 21.9% in the presence of 5 and 10 μM NAC, respectively, compared to the pure OVA, respec

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