Abstract
In conclusion, the interaction between the Strep-tagII and anti-Strep-tagII was explored at the single molecular level. Strep-tagII in the two-dimensional crystalline S-layer protein lattices on a silicon surface could be detected by anti-Strep-tagII antibodies coupled to AFM tip using single-molecule force spectroscopy. The unbinding force between Strep-tagII peptide and anti-Strep-tagII antibody was 27 pN at a loading rate of 177 pNs1.
Original language | English |
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Pages (from-to) | 2323-2326 |
Number of pages | 4 |
Journal | ChemPhysChem |
Volume | 11 |
DOIs | |
Publication status | Published - 2011 |
Fields of science
- 103036 Theoretical physics
- 211904 Biomechanics
- 103020 Surface physics
- 210 Nanotechnology
- 104010 Macromolecular chemistry
- 106006 Biophysics
- 106022 Microbiology
- 106048 Animal physiology
- 209 Industrial Biotechnology
- 304 Medical Biotechnology
- 404 Agricultural Biotechnology, Food Biotechnology
- 106049 Ultrastructure research
- 103021 Optics
- 106002 Biochemistry
- 104017 Physical chemistry
- 208 Environmental Biotechnology
- 104014 Surface chemistry
- 106023 Molecular biology
- 107 Other Natural Sciences
- 301110 Physiology
- 301206 Pharmacology
- 206 Medical Engineering
- 301306 Medical molecular biology
- 302044 Medical physics
- 301902 Immunology
- 305910 Traffic medicine
JKU Focus areas
- Engineering and Natural Sciences (in general)