- Observation of photoactive yellow protein anchored to a modified Au(1 1 1) surface by scanning tunneling microscopy
- Chemical Physics Letters
- Volume | Issue number
- 472 | 1-3
- Pages (from-to)
- Document type
- Faculty of Science (FNWI)
- Swammerdam Institute for Life Sciences (SILS)
The adsorption of photoactive yellow protein (PYP) on a Au(1 1 1) surface and its fluorescence activity have been studied by electrochemical scanning tunneling microscopy (EC-STM) and fluorescence photometry. A stable, densely packed protein layer was observed after protein immobilization onto a Au(1 1 1) surface modified with a mixture of 3-mercaptopropanoic acid (3-MPA) and 11-mercaptoundecanoic acid (11-MUA) and subsequent formation of the amide bond with the use of N-hydroxysuccinimide and carbodiimide. Fluorescence photometry data indicate that covalent binding of PYP to the functionalized Au(1 1 1) surface does not interfere with the fluorescence properties of the native protein.
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