期刊
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
卷 35, 期 1, 页码 72-78出版社
SPRINGER
DOI: 10.1007/s00249-005-0010-1
关键词
molecular recognition; SPR; AFM; suicide coupler; hAGT; SNAP-tag
类别
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.
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