| 1. |
- Fornander, Louise Helena, et al.
(author)
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Using Nanofluidic Channels to Probe the Dynamics of Rad51-DNA Filaments
- 2014
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In: Biophysical Journal. - : Elsevier BV. - 0006-3495 .- 1542-0086. ; 106:2, s. 692A-693A
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Journal article (other academic/artistic)abstract
- Rad51 is a key protein involved in the strand exchange reaction, a reaction where genetic material is transferred between two homologous DNA strands. Strand exchange is initiated by Rad51 forming a helical filament around single-stranded DNA (ssDNA), and the strand exchange is thereafter executed with a homologous double-stranded DNA (dsDNA). The structure of Rad51-DNA filaments, and also the activity of the strand exchange reaction, is dependent on the presence of ATP and dications, where Ca2+ has been shown to promote a higher degree of strand exchange than Mg2+.
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| 2. |
- Frykholm, Karolin, et al.
(author)
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Probing Physical Properties of a DNA-Protein Complex Using Nanofluidic Channels
- 2014
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In: Biophysical Journal. - : Elsevier BV. - 0006-3495 .- 1542-0086. ; 106:2, s. 428A-429A
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Journal article (other academic/artistic)abstract
- Nanofluidic channels have become an important tool to investigate single DNA molecules both from a fundamental polymer physics perspective as well as in e.g. optical mapping techniques. However, less effort has been made to study DNA-protein complexes. A main reason is that the extreme surface-to-volume ratio in the nanochannels causes most proteins to stick to the channel walls. We have recently overcome this problem by coating the channels with a lipid bilayer, thereby eliminating sticking.
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| 3. |
- Frykholm, Karolin, 1977, et al.
(author)
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Probing Physical Properties of a DNA- Protein Complex Using Nanofluidic Channels
- 2014
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In: Small. - : Wiley. - 1613-6810 .- 1613-6829. ; 10:5, s. 884-887
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Journal article (peer-reviewed)abstract
- A method to investigate physical properties of a DNA-protein complex in solution is demonstrated. By using tapered nanochannels and lipid passivation the persistence length of a RecA filament formed on double-stranded DNA is determined to 1.15 μm, in agreement with the literature, without attaching protein or DNA to any handles or surfaces.
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