Using nanofluidic channels to probe dynamics of RAD51-Filaments
Paper in proceedings, 2015

Using nanochannels, passivated with a lipid bilayer to avoid sticking of proteins, we study Rad51 filaments bound to single- and double stranded DNA. We demonstrate how we can discern different properties of the filaments by studying them at different degrees of confinement. Unlike the bacterial homologue RecA, that forms homogeneous filaments along DNA, Rad51 forms heterogeneous filaments containing both rigid kinks as well as flexible regions. Varying the counterion, the DNA substrate as well as the initial protein concentration, we try to understand the factors governing the structure of the filaments.

DNA-protein interactions

Nanofluidics

Rad51

Lipid passivation

Author

Louise Fornander

Chalmers, Chemistry and Chemical Engineering, Chemistry and Biochemistry, Physical Chemistry

Other publications Research

Mohammadreza Alizadehheidari

Chalmers, Chemistry and Chemical Engineering, Chemistry and Biochemistry, Physical Chemistry

Other publications Research

E. Werner

University of Gothenburg

A. Çekir

University of Gothenburg

Joachim Fritzsche

Chalmers, Applied Physics, Chemical Physics

Other publications Research

J. Araya

Northeastern University

P. Nevin

Northeastern University

P. J. Beuning

Northeastern University

Bernhard Mehlig

University of Gothenburg

M. Modesti

Aix Marseille University

Karolin Frykholm

Chalmers, Biology and Biological Engineering, Chemical Biology

Other publications Research

F. Persson

Uppsala University

Fredrik Westerlund

Chalmers, Chemistry and Chemical Engineering, Chemistry and Biochemistry, Physical Chemistry

Other publications Research

18th International Conference on Miniaturized Systems for Chemistry and Life Sciences, MicroTAS 2014

1826-1828

Areas of Advance

Nanoscience and Nanotechnology (2010-2017)

Life Science Engineering (2010-2018)

Subject Categories

Biochemistry and Molecular Biology

ISBN

978-097980647-6

More information

Latest update

4/4/2018 6

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