Related Experiment Video

Updated: Aug 15, 2026

Ensemble Force Spectroscopy by Shear Forces
07:30

Ensemble Force Spectroscopy by Shear Forces

Published on: July 26, 2022

Spin state and unfolding equilibria of ferricytochrome c in acidic solutions

H J Dyson, J K Beattie

    The Journal of Biological Chemistry
    |March 10, 1982
    PubMed

    More Related Videos

    Magnetometric Characterization of Intermediates in the Solid-State Electrochemistry of Redox-Active Metal-Organic Frameworks06:53

    Magnetometric Characterization of Intermediates in the Solid-State Electrochemistry of Redox-Active Metal-Organic Frameworks

    Published on: June 9, 2023

    Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers09:33

    Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

    Published on: March 21, 2025

    Related Concept Videos

    Protein Folding01:22

    Protein Folding

    Overview
    Colors and Magnetism03:02

    Colors and Magnetism

    Color in Coordination Complexes
    When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human eye.
    Molecular Chaperones and Protein Folding03:00

    Molecular Chaperones and Protein Folding

    The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
    The...
    Protein Folding01:25

    Protein Folding

    Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
    Protein Structure Is Critical to Its Biological Function
    Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
    Electron Transport Chain: Complex III and IV01:43

    Electron Transport Chain: Complex III and IV

    During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
    Microbes and Other Elemental Cycles01:24

    Microbes and Other Elemental Cycles

    Microbial activity plays a pivotal role in the biogeochemical cycling of iron and manganese, especially at the redox gradients characteristic of stratified aquatic environments. These cycles are driven by microbial transformations between oxidized and reduced forms of the metals, allowing organisms to exploit them for metabolic energy and structural purposes.Iron Cycling Across Redox GradientsIn neutral, oxygen-rich surface waters, iron is predominantly found in its oxidized, insoluble ferric...