Hydrodynamic interactions in DNA thermophoresis
Related Experiment Video
Updated: Feb 16, 2026

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions
Published on: February 10, 2022
1Laboratoire Ondes et Matière d'Aquitaine, Université de Bordeaux & CNRS, 33405 Talence, France. alois.wurger@u-bordeaux.fr.
Abstract:
We theoretically study the molecular-weight dependence of DNA thermophoresis, which arises from mutual advection of the n repeat units of the molecular chain. As a main result we find that the dominant driving forces, i.e., the thermally induced permittivity gradient and the electrolyte Seebeck effect, result in characteristic hydrodynamic screening. In comparison with recent experimental data on single-stranded DNA (2 ≤ n ≤ 80), our theory provides a good description for the increase of the drift velocity up to n = 30; the slowing-down of longer molecules is well accounted for by a simple model for counterion condensation. It turns out that thermophoresis may change sign as a function of n: for an appropriate choice of the salt-specific Seebeck coefficient, short molecules move to the cold and long ones to the hot; this could be used for separating DNA by molecular weight.
Related Concept Videos
Translesion DNA Polymerases
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
DNA Topoisomerases
Types and Mechanism of action
Topoisomerases are divided into two main types. ...
DNA Helicases
Recombinant DNA
DNA Replication
Replication in Prokaryotes
DNA replication...
DNA-only Transposons
The donor site from where the transposon is excised is either degraded or...

