Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Identification of chalcopyrite-binding peptides for flotation applications using phage display and deep sequencing.

Journal of biotechnology·2026
Same author

From Ultrafast Photoinduced Small Polarons to Cooperative and Macroscopic Charge-Transfer Phase Transition.

Angewandte Chemie (International ed. in English)·2024
Same author

Game-based training to improve the compliance of hospital pharmacy operators with handwashing guidelines.

The Journal of hospital infection·2023
Same author

The Wood equation allows consistent fitting of individual antibody-response profiles of Zika virus or SARS-CoV-2 infected patients.

Heliyon·2023
Same author

Already low drug dose antagonism of the renin-angiotensin aldosterone system decreases 1-year mortality and rehospitalization in old heart failure patients.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2022
Same author

Necrotizing myopathy associated with TET2-mutated myelodysplastic syndrome.

QJM : monthly journal of the Association of Physicians·2022

Related Experiment Video

Updated: Feb 20, 2026

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

1.5K

Ceruloplasmin-anion interaction. A circular dichroism spectroscopic study

M Herve, A Garnier, L Tosi

    Biochimica Et Biophysica Acta
    |August 9, 1976
    PubMed
    Summary

    Anion binding to ceruloplasmin (Cp) alters its spectral properties, disrupting copper-sulfur bonds. This study reveals simultaneous anion binding, bond disruption, and copper coordination in ceruloplasmin.

    More Related Videos

    Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
    11:38

    Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

    Published on: April 5, 2022

    3.0K
    IridiumIII Luminescent Probe for Detection of the Malarial Protein Biomarker Histidine Rich Protein-II
    12:52

    IridiumIII Luminescent Probe for Detection of the Malarial Protein Biomarker Histidine Rich Protein-II

    Published on: July 7, 2015

    9.7K

    Related Experiment Videos

    Last Updated: Feb 20, 2026

    Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
    09:33

    Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

    Published on: March 21, 2025

    1.5K
    Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
    11:38

    Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

    Published on: April 5, 2022

    3.0K
    IridiumIII Luminescent Probe for Detection of the Malarial Protein Biomarker Histidine Rich Protein-II
    12:52

    IridiumIII Luminescent Probe for Detection of the Malarial Protein Biomarker Histidine Rich Protein-II

    Published on: July 7, 2015

    9.7K

    Area of Science:

    • Biochemistry
    • Spectroscopy
    • Protein Chemistry

    Background:

    • Ceruloplasmin (Cp) is a key copper-containing protein involved in various biological processes.
    • Understanding anion interactions with Cp is crucial for elucidating its structure-function relationship.

    Purpose of the Study:

    • To investigate the effects of specific anion binding on the spectral characteristics of ceruloplasmin.
    • To determine the molecular mechanisms underlying anion-induced spectral changes in ceruloplasmin.

    Main Methods:

    • Absorption spectroscopy
    • Circular dichroism (CD) spectroscopy
    • Analysis of spectral data at varying anion concentrations.

    Main Results:

    • Anion binding (OCN-, N3-, SCN-) induced significant alterations in Cp's CD and absorption spectra.
    • Disappearance of positive bands and appearance of new negative bands in CD spectra were observed.
    • A decrease in absorption at 610 nm suggests disruption of a type I Cu-S(cysteine) bond, potentially due to protein secondary structure changes.
    • A new band at 410 nm indicates a charge transfer transition from a replacing ligand.
    • Isobestic points in spectra signify simultaneous anion binding, Cu-S bond disruption, and copper coordination.

    Conclusions:

    • Anion binding to ceruloplasmin triggers simultaneous structural and electronic changes.
    • The observed spectral shifts are attributed to the disruption of a type I Cu-S bond and subsequent coordination of copper to another protein residue.
    • These findings provide insights into the dynamic nature of ceruloplasmin's active site and its response to ligand interactions.