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Ligand-directed immobilization of proteins through an esterase 2 fusion tag studied by atomic force microscopy

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dc.title Ligand-directed immobilization of proteins through an esterase 2 fusion tag studied by atomic force microscopy en
dc.contributor.author Minařík, Antonín
dc.contributor.author Humeník, Martin
dc.contributor.author Li, Sheng
dc.contributor.author Huang, Yiwei
dc.contributor.author Krausch, Georg
dc.contributor.author Sprinzl, Mathias
dc.relation.ispartof Chembiochem
dc.identifier.issn 1439-4227 OCLC, Ulrich, Sherpa/RoMEO, JCR
dc.date.issued 2008-01-04
utb.relation.volume 9
utb.relation.issue 1
dc.citation.spage 124
dc.citation.epage 130
dc.type article
dc.language.iso en
dc.publisher Wiley-VCH Verlag GmbH & Co. en
dc.identifier.doi 10.1002/cbic.200700409
dc.relation.uri http://onlinelibrary.wiley.com/doi/10.1002/cbic.200700409/abstract
dc.subject atomic force microscopy en
dc.subject esterases en
dc.subject immobilization en
dc.subject inhibitors en
dc.subject site specificity en
dc.description.abstract Atomically flat mica surfaces were chemically modified with an alkyl trifluoromethyl ketone, a covalent inhibitor of esterase 2 from Alicyclobacillus acidocaldarius, which served as a tag for ligand-directed immobilization of esterase-linked proteins. Purifled NADH oxidase from Thermus thermophilus and human exportin-t from cell lysates were anchored on the modified surfaces. The immobilization effectiveness of the proteins was studied by atomic force microscopy (AFM). It was shown that ligand-esterase interaction allowed specific attachment of exportin-t and resulted in high-resolution images and coverage patterns that were comparable with immobilized purified protein. Moreover, the biological functionality of immobilized human exportin-t in forming a quaternary complex with tRNA and the GTPase Ran-GTP, and the dimension changes before and after complex formation were also determined by AFM. en
utb.faculty Faculty of Technology
dc.identifier.uri http://hdl.handle.net/10563/1002116
utb.identifier.obdid 43856710
utb.identifier.scopus 2-s2.0-38149071561
utb.identifier.wok 000252292200019
utb.identifier.pubmed 18046684
utb.identifier.coden CBCHF
utb.source j-wok
dc.date.accessioned 2011-08-16T15:06:30Z
dc.date.available 2011-08-16T15:06:30Z
utb.contributor.internalauthor Minařík, Antonín
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