Temperature dependence of unbinding forces between complementary DNA strands.
Force probe techniques such as atomic force microscopy can directly measure the force required to rupture single biological ligand receptor bonds. Such forces are related to the energy landscape of these weak, noncovalent biological interactions. We report unbinding force measurements between complementary strands of DNA as a function of temperature. Our measurements emphasize the entropic contributions to the energy landscape of the bond.
Schumakovitch
Irina
I
Department of Physics and Astronomy, National Center of Competence in Research on Nanoscale Science, University of Basel, CH-4056 Basel, Switzerland.
Grange
Wilfried
W
Strunz
Torsten
T
Bertoncini
Patricia
P
Güntherodt
Hans-Joachim
HJ
Hegner
Martin
M
D001483:Base Sequence; D018076:DNA, Complementary / Q000737:chemistry*; D018625:Microscopy, Atomic Force / Q000379:methods; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D011336:Probability; D013696:Temperature; D013816:Thermodynamics
D018076:DNA, Complementary; D009838:Oligodeoxyribonucleotides