Stretching and immobilization of DNA for studies of protein–DNA interactions at the single-molecule level

Kim, JiHoon; Dukkipati, VenkatRam; Pang, Stella W; Larson, Ronald G

doi:10.1007/s11671-007-9057-5

Stretching and immobilization of DNA for studies of protein–DNA interactions at the single-molecule level

Nano Review
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Published: 18 April 2007

Volume 2, article number 185, (2007)
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Stretching and immobilization of DNA for studies of protein–DNA interactions at the single-molecule level

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JiHoon Kim¹,
VenkatRam Dukkipati²,
Stella W Pang² &
…
Ronald G Larson¹

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Abstract

Single-molecule studies of the interactions of DNA and proteins are important in a variety of biological or biotechnology processes ranging from the protein’s search for its DNA target site, DNA replication, transcription, or repair, and genome sequencing. A critical requirement for single-molecule studies is the stretching and immobilization of otherwise randomly coiled DNA molecules. Several methods for doing so have been developed over the last two decades, including the use of forces derived from light, magnetic and electric fields, and hydrodynamic flow. Here we review the immobilization and stretching mechanisms for several of these techniques along with examples of single-molecule DNA–protein interaction assays that can be performed with each of them.

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Department of Chemical Engineering, University of Michigan, Ann Arbor, 48109, MI, USA
JiHoon Kim & Ronald G Larson
Department of Electrical Engineering and Computer Science, University of Michigan, Ann Arbor, 48109, MI, USA
VenkatRam Dukkipati & Stella W Pang

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JiHoon Kim
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VenkatRam Dukkipati
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Stella W Pang
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Ronald G Larson
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Kim, J., Dukkipati, V., Pang, S.W. et al. Stretching and immobilization of DNA for studies of protein–DNA interactions at the single-molecule level. Nanoscale Res Lett 2, 185 (2007). https://doi.org/10.1007/s11671-007-9057-5

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Received: 13 March 2007
Accepted: 30 March 2007
Published: 18 April 2007
DOI: https://doi.org/10.1007/s11671-007-9057-5

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Stretching and immobilization of DNA for studies of protein–DNA interactions at the single-molecule level

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