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Originally published as Biophys J. BioFAST on August 31, 2004.
doi:10.1529/biophysj.104.039776
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Biophysical Journal 87:3388-3396 (2004)
© 2004 The Biophysical Society

Dynamics of the DNA Duplex Formation Studied by Single Molecule Force Measurements

U. Bockelmann, P. Thomen and F. Heslot

Laboratoire Pierre Aigrain, Ecole Normale Supérieure, Paris, France

Correspondence: Address reprint requests to Ulrich Bockelmann, E-mail: ulrich{at}lpa.ens.fr.

DNA is partly denatured in vitro by applying a force that mechanically separates the two strands of the double helix. Sudden reduction of the imposed displacement triggers spontaneous reannealing of the molecule. The corresponding force signals are measured by optical trapping interferometry for backward steps of various amplitudes and base sequence intervals. The measured signals frequently show plateaus of varying duration at discrete values that are dependent on the base sequence. Additional measurements are performed with proteins bound to the double helix. When the opening fork encounters such a protein during mechanical unzipping, force increases until the protein is ejected. This ejection induces fast release of tension and fast unzipping. Comparing our different measurements, we find that both DNA unzipping and the relaxation of tension in DNA are faster than the formation of the double helix.




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U. Bockelmann and V. Viasnoff
Theoretical Study of Sequence-Dependent Nanopore Unzipping of DNA
Biophys. J., April 1, 2008; 94(7): 2716 - 2724.
[Abstract] [Full Text] [PDF]




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