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Nanoscale “Curtain Rods”: High-Throughput Tools for Studying DNA-Protein Interactions

Published online by Cambridge University Press:  01 February 2011

Teresa Fazio ,
Mari-Liis Visnapuu ,
Shalom J. Wind  and
Eric Greene
Teresa Fazio
Affiliation:
taf2102@columbia.edu, Columbia University, Applied Physics and Applied Mathematics, New York, New York, United States
Mari-Liis Visnapuu
Affiliation:
mv2192@columbia.edu, Columbia University, Biochemistry and Molecular Biophysics, New York, New York, United States
Shalom J. Wind
Affiliation:
sw2128@columbia.edu, Columbia University, Applied Physics and Applied Mathematics, New York, New York, United States
Eric Greene
Affiliation:
ecg2108@columbia.edu, Columbia University, New York, New York, United States
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Abstract

In this work, we combine nanoscale engineering with single-molecule biology to probe the biochemical interactions between individual proteins and DNA. This approach, a vast improvement over previous methods, constructs a platform to observe thousands of protein-DNA interactions in real time with unprecedented detail. A key challenge in these experiments involves collecting enough statistically relevant data in order to analyze reactions which are designed to be probed individually. “DNA curtains” are formed by flowing the DNA tethered to a lipid bilayer across nanopatterned barriers, facilitating massively parallel data acquisition.

Keywords

nanoscalebiomedicaldevices
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1138: Symposium FF – Nanofunctional Materials, Structures and Devices for Biomedical Applications , 2008 , 1138-FF08-03
Copyright
Copyright © Materials Research Society 2009

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References

REFERENCES

1. Graneli, A., Yeykal, C., Robertson, R.B., & Greene, E.C., Proceedings of the National Academy of Sciences, USA 103, 1221–1226 (2006).Google Scholar
2. Gorman, J., Chowdhury, A., Surtees, J.A., Shimada, J., Reichman, D.R., Alani, E., & Greene, E.C., Mol Cell 28, 359–370 (2007).Google Scholar
3. Graneli, A., Yeykal, C., Prasad, T.K., & Greene, E.C., Langmuir 22, 292–299 (2006).Google Scholar
4. Yeykal, C. C., Greene, E.C., Cell Cycle 5 (10), 1033–1038 (2006).Google Scholar
5. Sackmann, E., Science 271, 43–48 (1996).Google Scholar
6. Cremer, P. S., & Boxer, S.G., J. Phys. Chem. B 103, 2554–2559 (1999).Google Scholar
7. Fazio, T. A., Visnapuu, M.L., Wind, S.J., and Greene, E.C., Langmuir 24 (18), 10524–10531 (2008).Google Scholar
8. Visnapuu, M. L., Fazio, T.A., Wind, S.J., Greene, E.C., Langmuir 24 (19), 11293–11299 (2008).Google Scholar
9. Avanti, . Polar Lipids.Google Scholar
10. Tsai, J., Sun, E., Gao, Y., Hone, J. C., and Kam, L.C., Nano Letters 8 (2), 425–430 (2008).Google Scholar