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dc.contributor.authorLiu, Tseng-Huangen_US
dc.contributor.authorHuang, Yun-Tzuen_US
dc.contributor.authorCheng, Hui-Wenen_US
dc.contributor.authorChen, Yen-Weien_US
dc.contributor.authorLee, Ching-Hungen_US
dc.contributor.authorHsu, Yu-Dien_US
dc.contributor.authorPan, Rong-Longen_US
dc.contributor.authorTseng, Fan-Gangen_US
dc.date.accessioned2015-12-02T02:59:30Z-
dc.date.available2015-12-02T02:59:30Z-
dc.date.issued2015-09-10en_US
dc.identifier.issn1932-7447en_US
dc.identifier.urihttp://dx.doi.org/10.1021/acs.jpcc.5b05944en_US
dc.identifier.urihttp://hdl.handle.net/11536/128280-
dc.description.abstractManipulating a single protein molecule on liposomes or planar lipid bilayers is a useful technique for studying membrane-bound proteins, receptors, or ion transporters and for delicate applications including biosensor chips, drug screening, and clinical diagnoses. However, several key breakthroughs are required for success through difficult techniques such as single protein take-and-place with reasonable spatiotemporal control. In this report, a novel method was established for placing a single transmembrane protein onto a patterned lipid bilayer. A surface-functionalized 1.8 nm gold nanoparticle was first engineered at the tip of an atomic force microscope. A single transmembrane protein, H+-translocating pyrophosphatase with six-histidine residues tag, was then picked up using such a microscopy tip where its nanoparticle was modified by nickel-nitrilotriacetic acid. Two-step fluorescence bleaching observation and quantum dot blinking analysis subsequently verified successful manipulation of a single functional protein on a lipid membrane in a predetermined manner. Furthermore, the enzymatic activity from the single H+-translocating pyrophosphatase was determined, demonstrating that membrane proteins retain their functions on the lipid bilayer through a single-molecule take-and-place technique. This innovative technique overcomes current limitations and provides a single biomolecule nanomanipulation system for versatile studies of membrane-bound proteins.en_US
dc.language.isoen_USen_US
dc.titleSingle Molecule Take-and-Place Technique for Positioning a Membrane Protein on a Lipid Bilayeren_US
dc.typeArticleen_US
dc.identifier.doi10.1021/acs.jpcc.5b05944en_US
dc.identifier.journalJOURNAL OF PHYSICAL CHEMISTRY Cen_US
dc.citation.volume119en_US
dc.citation.issue36en_US
dc.citation.spage21184en_US
dc.citation.epage21190en_US
dc.contributor.department奈米科技中心zh_TW
dc.contributor.departmentCenter for Nanoscience and Technologyen_US
dc.identifier.wosnumberWOS:000361255100045en_US
dc.citation.woscount0en_US
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