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

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

You might also read

Related Articles

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

Sort by
Same author

Following phospholipid transfer through the OmpF<sub>3</sub>-MlaA-MlaC lipid shuttle with native mass spectrometry.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Membrane Protein Complexity Revealed Through Native Mass Spectrometry.

Annual review of biochemistry·2025
Same author

Traversing the drug discovery landscape using native mass spectrometry.

Current opinion in structural biology·2025
Same author

Defining proteoform-specific interactions for drug targeting in a native cell signalling environment.

Nature chemistry·2025
Same author

Structural insights into the high basal activity and inverse agonism of the orphan receptor GPR6 implicated in Parkinson's disease.

Science signaling·2024
Same author

Coupling and Activation of the β1 Adrenergic Receptor - The Role of the Third Intracellular Loop.

Journal of the American Chemical Society·2024

Related Experiment Video

Updated: Jun 11, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

When proteomics meets structural biology.

Min Zhou1, Carol V Robinson

  • 1Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ , UK.

Trends in Biochemical Sciences
|July 15, 2010
PubMed
Summary
This summary is machine-generated.

Mass spectrometry (MS) integrates proteomics and structural biology data to map protein interactions and modifications. This approach provides crucial context for understanding protein function within 3D structural models.

More Related Videos

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Related Experiment Videos

Last Updated: Jun 11, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Area of Science:

  • Biochemistry
  • Structural Biology
  • Proteomics

Background:

  • Proteomics has identified numerous interacting proteins and their post-translational modifications.
  • Integrating this data with structural biology and homology modeling to provide context for modifications remains a challenge.

Purpose of the Study:

  • To review the application of mass spectrometry (MS) in integrating proteomics and structural biology data.
  • To highlight how MS can provide topological and atomic context for protein modifications and interactions.

Main Methods:

  • Utilizing MS-based approaches to analyze subunit stoichiometry in protein complexes.
  • Applying MS to define protein interaction networks and subunit packing.
  • Superimposing proteomics data onto low-resolution 3D models and high-resolution atomic structures.

Main Results:

  • MS enables the definition of subunit stoichiometry, interaction networks, and subunit packing.
  • This integration facilitates the generation of 3D models for protein complexes.
  • Overlaying proteomics data onto structural models offers new functional insights.

Conclusions:

  • Mass spectrometry is a key technology bridging proteomics and structural biology.
  • Integrating diverse data types through MS enhances understanding of protein complex structure and function.