Related Experiment Video
Updated: Jun 20, 2025

Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques
Published on: September 6, 2024
Tethered Particle Motion Analysis of DNA-Binding Properties of Architectural Proteins
Ramon A van der Valk1, Ilias Zarguit1, Niels Laurens2,3
1Leiden Institute of Chemistry, Leiden University, Leiden, The Netherlands.
Abstract:
Architectural DNA-binding proteins are key to the organization and compaction of genomic DNA inside cells. Tethered particle motion (TPM) permits analysis of DNA conformation and detection of changes in conformation induced by such proteins at the single molecule level in vitro. As many individual protein-DNA complexes can be investigated in parallel, these experiments have high throughput. TPM is therefore well suited for characterization of the effects of protein-DNA stoichiometry and changes in physicochemical conditions (pH, osmolarity, and temperature). Here, we describe in detail how to perform tethered particle motion experiments on complexes between DNA and architectural proteins to determine their structural and biochemical characteristics.
Related Concept Videos
Mechanical Protein Functions
Nucleosome Remodeling
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
DNA Helicases

