Related Experiment Video

Updated: Aug 6, 2026

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
08:07

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Published on: January 17, 2025

[Kinetic, energetic and stereochemical factors determining molecular recognition of proteins and nucleic acids]

V I Lim, V G Kliashtornyĭ

    Molekuliarnaia Biologiia
    |August 18, 2006
    PubMed

    More Related Videos

    The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis19:16

    The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

    Published on: March 17, 2010

    Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions06:50

    Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

    Published on: January 26, 2024

    Related Concept Videos

    Noncovalent Attractions in Biomolecules02:35

    Noncovalent Attractions in Biomolecules

    Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
    Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
    Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
    Noncovalent Attractions in Biomolecules02:35

    Noncovalent Attractions in Biomolecules

    Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
    Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
    Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
    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:
    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:
    Protein-protein Interfaces02:04

    Protein-protein Interfaces

    Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
    Ligand Binding Sites02:40

    Ligand Binding Sites

    Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
    Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...