Unknown

Dataset Information

0

Rapid internal contraction boosts DNA friction.

ABSTRACT: Macroscopic objects are usually manipulated by force and observed with light. On the nanoscale, however, this is often done oppositely: individual macromolecules are manipulated by light and monitored with force. This procedure, which is the basis of single-molecule force spectroscopy, has led to much of our quantitative understanding of how DNA works, and is now routinely applied to explore molecular structure and interactions, DNA-protein reactions and protein folding. Here we develop the technique further by introducing a dynamic force spectroscopy set-up for a non-invasive inspection of the tension dynamics in a taut strand of DNA. The internal contraction after a sudden release of the molecule is shown to give rise to a drastically enhanced viscous friction, as revealed by the slow relaxation of an attached colloidal tracer. Our systematic theory explains the data quantitatively and provides a powerful tool for the rational design of new dynamic force spectroscopy assays.

SUBMITTER: Otto O 

PROVIDER: S-EPMC3644107 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Rapid internal contraction boosts DNA friction.

Otto Oliver O   Sturm Sebastian S   Laohakunakorn Nadanai N   Keyser Ulrich F UF   Kroy Klaus K  

Nature communications 20130101

Macroscopic objects are usually manipulated by force and observed with light. On the nanoscale, however, this is often done oppositely: individual macromolecules are manipulated by light and monitored with force. This procedure, which is the basis of single-molecule force spectroscopy, has led to much of our quantitative understanding of how DNA works, and is now routinely applied to explore molecular structure and interactions, DNA-protein reactions and protein folding. Here we develop the tech  ...[more]