Related Experiment Video

Updated: Jul 6, 2026

Ensemble Force Spectroscopy by Shear Forces
07:30

Ensemble Force Spectroscopy by Shear Forces

Published on: July 26, 2022

Influence of ionic strength on Hoechst 33258 binding with DNA

Poghos O Vardevanyan1, Ara P Antonyan, Marine A Parsadanyan

  • 1Department of Biophysics, Yerevan State University, Yerevan, 375025, Armenia.

Journal of Biomolecular Structure & Dynamics
|April 11, 2008
PubMed
Summary

Hoechst 33258 binding to DNA changes significantly with ionic strength, revealing multiple interaction types. High ionic strength promotes high-affinity binding, unlike low ionic strength where sequence specificity is lost.

More Related Videos

Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks12:19

Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks

Published on: November 10, 2016

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy06:38

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy

Published on: February 7, 2019

Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
DNA Agarose Gel Electrophoresis02:35

DNA Agarose Gel Electrophoresis

Agarose gel electrophoresis is a laboratory technique commonly used to separate DNA fragments by size. However, it can also be used to isolate and purify DNA fragments using a gel extraction protocol.
Gel extraction follows five major steps: running gel electrophoresis to separate fragments, isolating the individual bands, extracting DNA from those bands, and removing the dye and salts from the extracted mixture to obtain pure DNA.
In cloning experiments, both the insert and vector DNA...
Theory of Strong Electrolytes01:23

Theory of Strong Electrolytes

The interionic forces of the strong electrolytes depend on the solvent's dielectric constant, which is the ability of a solvent to store electrical energy, based on its polarizability. and the solution's concentration. In high-dielectric solvents and in dilute solutions, weak electrostatic forces keep ions apart. However, in low-dielectric solvents or concentrated solutions, stronger interionic forces may cause ions to pair up as ionic doublets despite being fully ionized. The theory of strong...
Factors Affecting Activity Coefficient01:17

Factors Affecting Activity Coefficient

The extended Debye-Hückel equation indicates that the activity coefficient of an ion in an aqueous solution at 25°C depends on three partially interdependent properties: the ionic strength of the solution, the charge of the ion, and the ion size. 
The activity coefficient value for an ion is close to one when the solution has almost zero ionic strength, i.e., when the solution shows close to ideal behavior. As the ionic strength of the solution increases from 0 to 0.1 mol/L, a decrease in the...
Polyprotic Acids03:38

Polyprotic Acids

Acids are classified by the number of protons per molecule that they can give up in a reaction. Acids such as HCl, HNO3, and HCN that contain one ionizable hydrogen atom in each molecule are called monoprotic acids. Their reactions with water are:
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium: