| Literature DB >> 16160825 |
Stefan K Kufer1, Hendrik Dietz, Christian Albrecht, Kerstin Blank, Angelika Kardinal, Matthias Rief, Hermann E Gaub.
Abstract
A genetically modified form of the human DNA repair protein O(6)-alkylguanine-DNA-alkyltransferase (hAGT) was used to immobilize different recombinant hAGT fusion proteins covalently and selectively on gold and glass surfaces. Fusion proteins of hAGT with Glutathione S-Transferase and with tandem repeats of Titin Ig-domains, were produced and anchored via amino-polyethylene glycol benzylguanine. Anchoring was characterized and quantified with surface plasmon resonance, atomic force microscope and fluorescence measurements. Individual fusion proteins were unfolded by single molecule force spectroscopy corroborating the selectivity of the covalent attachment.Entities:
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Year: 2005 PMID: 16160825 DOI: 10.1007/s00249-005-0010-1
Source DB: PubMed Journal: Eur Biophys J ISSN: 0175-7571 Impact factor: 1.733