Related Experiment Video

Updated: Aug 15, 2026

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water
16:24

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

Salt-induced transition between two double-helical forms of oligo (dC-dG)

F M Pohl

    Cold Spring Harbor Symposia on Quantitative Biology
    |January 1, 1983
    PubMed

    More Related Videos

    X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep105011:27

    X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

    Published on: May 13, 2020

    CD Spectroscopy to Study DNA-Protein Interactions06:48

    CD Spectroscopy to Study DNA-Protein Interactions

    Published on: February 10, 2022

    Related Concept Videos

    Cooperative Allosteric Transitions01:58

    Cooperative Allosteric Transitions

    Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
    DNA Topoisomerases02:02

    DNA Topoisomerases

    Topoisomerases are enzymes that relax overwound DNA molecules during various cell processes, including DNA replication and transcription. These enzymes regulate positive and negative DNA supercoiling without changing the nucleotide sequence. DNA overwinding in a clockwise direction results in positively supercoiled DNA, whereas underwinding in a counterclockwise direction produces negatively supercoiled DNA.
    Types and Mechanism of action
    Topoisomerases are divided into two main types.  Type I...
    Cooperative Allosteric Transitions01:58

    Cooperative Allosteric Transitions

    Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
    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...
    Cooperative Allosteric Transitions01:58

    Cooperative Allosteric Transitions

    Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
    Protein Denaturation01:28

    Protein Denaturation

    The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...