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- W2891707605 abstract "Thiol chemistry provides a way for proteins to alter their form and function rapidly and reversibly. Although a variety of bulk techniques have been developed to ascertain the oxidation state and bonding of cysteine thiols, these methods may destroy the sample or lead to unwanted side reactions. Single-molecule force spectroscopy harnesses the ability to track protein folding and unfolding pathways with angstrom precision to detect changes in thiol chemistry in a real-time and non-destructive manner. As the oxidation state of the thiol changes, owing to intramolecular disulfide bonding or post-translational modification, changes to the protein topology and stability can be detected by unfolding of single-protein domains using the atomic force microscope. Not only does this provide a means to probe the mechanism of covalent bond scission by small nucleophiles and enzymes, but also a tool by which to monitor the activity of single oxidoreductase molecules as they introduce and rearrange disulfide bonds while protein substrates fold. Although a carnivore's bite damages tissue by tearing apart molecular bonds, nature has provided enzymatic machinery to repair the bonds, a process that can be directly observed using single-molecule techniques." @default.
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- W2891707605 date "2018-01-01" @default.
- W2891707605 modified "2023-09-27" @default.
- W2891707605 title "CHAPTER 1.3. Real-time Detection of Thiol Chemistry in Single Proteins" @default.
- W2891707605 doi "https://doi.org/10.1039/9781788013253-00052" @default.
- W2891707605 hasPublicationYear "2018" @default.
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