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- W2025828429 abstract "Regulated and selective transport of biomolecules across biological membranes is mediated by transporter proteins. These are essential in physiological processes ranging from electrical signaling in the nervous system to secretion of hormones and maintenance of electrochemical gradients. Though transporters are extensively studied, there are currently no techniques available to investigate their function at the single molecule level. We have developed a fluorescence-based assay to monitor thousands of individual nanoscale proteoliposomes in parallel by immobilizing them on functionalized glass surfaces (1-5).We recently extended this assay to allow real-time observation of substrate translocation mediated by single transporters reconstituted into liposomes. Here we present the development of the assay including characterization and optimization of the most critical system components including: minimization of leakage, in situ real-time calibration of absolute transport rates and increase of photostability for long term recordings (∼40min). We also present high-resolution single molecule activity recordings of the transporter protein, Arabidopsis thaliana H+-ATPase (AHA2).References:1. Mathiasen et al., Nature Methods. (2014) 11:931-342. Christensen. et al. Nat Nanotechnol. (2012) 7:51-53. Hatzakis. et al. Nat. Chem. Biol. (2009) 5:835-414. Bendix. et al. PNAS. (2009) 106:12341-65. Kunding. et al. Biophys J. (2008) 95:1176-88" @default.
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- W2025828429 date "2015-01-01" @default.
- W2025828429 modified "2023-09-26" @default.
- W2025828429 title "Development of a Fluorescence-Based Assay for Functional Studies of Transporter Proteins on the Single Molecule Level" @default.
- W2025828429 doi "https://doi.org/10.1016/j.bpj.2014.11.1032" @default.
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