2002
DOI: 10.1016/s0006-3495(02)75416-7
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Temperature Dependence of Unbinding Forces between Complementary DNA Strands

Abstract: 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.

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Cited by 104 publications
(96 citation statements)
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References 24 publications
(30 reference statements)
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“…In particular, Schumakovitch et al [1156] have studied the temperature dependence of unbinding forces between complementary DNA strands. Sattin et al [1146] determined the force Fig.…”
Section: Rupture Force Of Specific Interactionsmentioning
confidence: 99%
“…In particular, Schumakovitch et al [1156] have studied the temperature dependence of unbinding forces between complementary DNA strands. Sattin et al [1146] determined the force Fig.…”
Section: Rupture Force Of Specific Interactionsmentioning
confidence: 99%
“…5.2.1). Similar experiments have been carried out to investigate the kinetics of short DNA hairpins using SMF [161,162] or AFM [163,164,165,166,167] finding slower kinetics of unfolding/refolding depending on the length of the sequence as predicted by some theoretical models [133,168]. Mechanical unfolding of single RNA molecules through nanopores has been also proposed as a method to determine the secondary structure [169].…”
Section: Rnamentioning
confidence: 98%
“…Strunz et al [7,8] investigated the unbinding of DNA duplex of various lengths and found that the unbinding force depends on the loading rate and sequence length. It was also found that changing the pulling direction results different unbinding forces [11,13].…”
Section: Introductionmentioning
confidence: 99%