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Personen: Minarik, Antonin (Autor) 
Humenik, Martin (Autor) 
Li, Sheng (Autor) 
Huang, Yiwei (Autor) 
Krausch, Georg (Autor) 
Sprinzl, Mathias (Autor) 
  
Titel: Ligand-directed immobilization of proteins through an esterase 2 fusion tag studied by atomic force microscopy
  
Quelle: Chembiochem : a European journal of chemical biology. Bd. 9. H. 1. S. 124 - 130
Erscheinungsjahr:    2008
ISBN / ISSN: 1439-7633
URL der Originalveröffentlichung doi:10.1002/cbic.200700409
  
Dokumentart:
Zeitschriftenaufsatz Zeitschriftenaufsatz
Sprache: Englisch
Open Access:
Person der Universität:    Krausch, Georg  In UnivIS suchen 
Einrichtung: Universitätsleitung
DDC-Sachgruppe:    Chemie
ID: 11071  Universitätsbibliothek Mainz
Hinweis:
Informationen zu den Nutzungsrechten unserer Inhalte Informationen zu den Nutzungsrechten unserer Inhalte
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. Purified 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.
   
  
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