Mechanisms of DNA binding determined in optical tweezers experiments
- 1 November 2006
- journal article
- review article
- Published by Wiley in Biopolymers
- Vol. 85 (2) , 154-168
- https://doi.org/10.1002/bip.20622
Abstract
The last decade has seen rapid development in single molecule manipulation of RNA and DNA. Measuring the response force for a particular manipulation has allowed the free energies of various nucleic acid structures and configurations to be determined. Optical tweezers represent a class of single molecule experiments that allows the energies and structural dynamics of DNA to be probed up to and beyond the transition from the double helix to its melted single strands. These experiments are capable of high force resolution over a wide dynamic range. Additionally, these investigations may be compared with results obtained when the nucleic acids are in the presence of proteins or other binding ligands. These ligands may bind into the major or minor groove of the double helix, intercalate between bases or associate with an already melted single strand of DNA. By varying solution conditions and the pulling dynamics, energetic and dynamic information may be deduced about the mechanisms of binding to nucleic acids, providing insight into the function of proteins and the utility of drug treatments. © 2006 Wiley Periodicals, Inc. Biopolymers 85:154–168, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.comKeywords
This publication has 145 references indexed in Scilit:
- Single DNA molecule stretching measures the activity of chemicals that target the HIV-1 nucleocapsid proteinAnalytical Biochemistry, 2006
- Exploring the Interaction of Ruthenium(II) Polypyridyl Complexes with DNA Using Single-Molecule TechniquesLangmuir, 2006
- Mechanistic Insights into the Kinetics of HIV-1 Nucleocapsid Protein-facilitated tRNA Annealing to the Primer Binding SiteJournal of Molecular Biology, 2004
- HIV-1 nucleocapsid protein activates transient melting of least stable parts of the secondary structure of TAR and its complementary sequenceJournal of Molecular Biology, 2002
- NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the Ψ-RNA packaging signal. implications for genome recognition 1 1Edited by P. WrightJournal of Molecular Biology, 2000
- Single molecule force spectroscopy in biology using the atomic force microscopeProgress in Biophysics and Molecular Biology, 2000
- Binding properties of the human immunodeficiency virus type 1 nucleocapsid protein p7 to a model RNA: elucidation of the structural determinants for function 1 1Edited by D. E. DraperJournal of Molecular Biology, 1999
- First Glimpses at Structure-function Relationships of the Nucleocapsid Protein of RetrovirusesJournal of Molecular Biology, 1995
- Ion effects on ligand-nucleic acid interactionsJournal of Molecular Biology, 1976
- Interaction between parallel rodlike macroionsBiopolymers, 1968