Fig. 3: Real-time kinetic analysis with a conformational sensor.
From: Nanopore sensing of protein and peptide conformation for point-of-care applications
a A protein (P) is trapped inside a pore by molecular trapping. Partner binding (B), results in a complex with a different conformation. The change in pore volume occupied by the complex or a change in conformation can be detected by a shift of blockade level (P + B) in real time. b 160Current trace, in real-time, of the capture of an engineered E. coli dihydrofolate reductase (DHFRtag) complexed with methotrexate (MTX), free or bound to NADPH or NADP+ inside a ClyA nanopore in 150 mM NaCl, 15 mM Tris HCl, pH 7,5. Reprinted (adapted) with permission from Soskine, M., et al. Single-Molecule Analyte Recognition with ClyA Nanopores Equipped with Internal Protein Adaptors. J. Am. Chem. Soc. 137, 5793–5797 (2015). Copyright 2015, American Chemical Society113. c) Current trace of the capture of SBD1 (substrate binding domain 1) and GBP (glucose binding protein) in a ClyA nanopore unbound, and bound to respectively, Asparagine and Glucose in a 100-fold dilution of sweat in 150 mM NaCl, 15 mM Tris HCl, pH 7,5. Figure adapted from Nature Com. Galenkamp et al.114. Created in BioRender. Ratinho, L. (2025) https://BioRender.com/v49u400.
