{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ju Z"],"funding":["National Natural Science Foundation of China"],"pagination":["e16711"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12948236"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(12)"],"pubmed_abstract":["Electronic transport properties of single proteins offer powerful insights into their structure and dynamics. However, the orientation variability of electrode-attached protein molecules poses a big difficulty in achieving precise electric measurements and reliable data interpretation. Here, a DNA origami-based method that promotes preferred orientations of target proteins is reported, enabling more reproducible single-molecule electrical characterization. With two orthogonal DNA aptamers installed inside a DNA origami nanocavity, a thrombin protein can be captured with a prescribed orientation between a gold substrate and a conductive AFM tip. Matrix-patterned I-V measurements reveal that bivalently anchored thrombin molecules exhibit significantly reduced conductance variability compared"],"journal":["Advanced science (Weinheim, Baden-Wurttemberg, Germany)"],"pubmed_title":["DNA-Guided Robust Single-Protein Electronic Readout."],"pmcid":["PMC12948236"],"funding_grant_id":["22434005"],"pubmed_authors":["Li Y","Li J","Ju Z","Deng Z"],"additional_accession":[]},"is_claimable":false,"name":"DNA-Guided Robust Single-Protein Electronic Readout.","description":"Electronic transport properties of single proteins offer powerful insights into their structure and dynamics. However, the orientation variability of electrode-attached protein molecules poses a big difficulty in achieving precise electric measurements and reliable data interpretation. Here, a DNA origami-based method that promotes preferred orientations of target proteins is reported, enabling more reproducible single-molecule electrical characterization. With two orthogonal DNA aptamers installed inside a DNA origami nanocavity, a thrombin protein can be captured with a prescribed orientation between a gold substrate and a conductive AFM tip. Matrix-patterned I-V measurements reveal that bivalently anchored thrombin molecules exhibit significantly reduced conductance variability compared","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-16T22:20:47.34Z","creation":"2026-07-11T03:12:14.446Z"},"accession":"S-EPMC12948236","cross_references":{"pubmed":["41405386"],"doi":["10.1002/advs.202516711"]}}