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 Experiment Videos

Sedimentation equilibrium studies.

Ian A Taylor1, John F Eccleston, Katrin Rittinger

  • 1Division of Protein Structure, National Institute for Medical Research, London, England, UK.

Methods in Molecular Biology (Clifton, N.J.)
|April 6, 2004
PubMed
Summary
This summary is machine-generated.

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

The E3-ome gene-centric compendium reveals the human E3 ligase landscape.

Cell·2026
Same author

Integrase anchors viral RNA to the HIV-1 capsid interior.

Nature·2026
Same author

Structure and mechanism of the HECT ligase HECTD3.

Nature communications·2026
Same author

Capsid flexibility during Ty1 virus-like particle assembly.

bioRxiv : the preprint server for biology·2025
Same author

KHNYN is a manganese-dependent endoribonuclease required for ZAP-mediated antiviral restriction.

Nucleic acids research·2025
Same author

Covalent fragment screening to inhibit the E3 ligase activity of bacterial NEL enzymes SspH1 and SspH2.

RSC chemical biology·2025
Same journal

Mapping the 3D Chromosome Organization of a Biosynthetic Gene Cluster by Capture Hi-C (CHi-C).

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Mapping the 3D Chromosome Organization of Streptomyces by Hi-C.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

CUT&Tag Epigenomic Profiling of Biosynthetic Gene Clusters in Arabidopsis thaliana.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Rhizobium rhizogenes-Mediated Hairy Root Transformation Protocol for Lotus japonicus and Other Legumes.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Characterization of Bioactive Saponins from Sea Cucumbers.

Methods in molecular biology (Clifton, N.J.)·2026
Same journal

Methods for Functional Validation of Terpenoid Metabolic Clusters in Nicotiana benthamiana and Aspergillus oryzae.

Methods in molecular biology (Clifton, N.J.)·2026
See all related articles

Understanding protein-protein interactions requires determining oligomerization states. Sedimentation equilibrium provides accurate molecular weights and association constants for self-associating systems, crucial for quantitative characterization.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Protein-protein interactions are vital for biological processes.
  • Accurate characterization necessitates understanding the oligomerization state of proteins.
  • Monomer-multimer self-association is a common phenomenon in biological systems.

Purpose of the Study:

  • To highlight the importance of determining oligomerization states for studying protein-protein interactions.
  • To present sedimentation equilibrium as a key method for quantitative analysis.
  • To demonstrate its utility in characterizing self-associating systems.

Main Methods:

  • Sedimentation equilibrium ultracentrifugation.
  • Determination of absolute solution molecular weight.

Related Experiment Videos

  • Analysis of monomer-multimer self-associating systems.

    • Main Results:

    • Sedimentation equilibrium yields reliable and accurate absolute molecular weights.
    • The method is independent of macromolecular shape.
    • Equilibrium constants for self-associating systems can be determined.

    Conclusions:

    • Sedimentation equilibrium is an ideal technique for characterizing protein oligomerization.
    • It provides essential data for quantitative analysis of protein-protein interactions.
    • This method is fundamental for understanding self-associating biological macromolecules.