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

Protein Digestion01:02

Protein Digestion

Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
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...
Protein Folding01:22

Protein Folding

Overview

You might also read

Related Articles

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

Sort by
Same author

Augmenting β2-adrenergic signaling during exercise to enhance anti-tumor immune function.

Exercise and sport sciences reviews·2026
Same author

Blinatumomab bypasses CD28 blockade to sustain T-cell cytotoxicity and improve survival in a xenograft B-ALL model.

Journal for immunotherapy of cancer·2026
Same author

Post-Transplant Bendamustine as a Platform for Immune Modulation After Allogeneic Hematopoietic Cell Transplantation.

European journal of haematology·2026
Same author

TIGIT Blockade Potentiates the Anti-Leukemic Activity of Exercise-Mobilized Donor Lymphocytes and Expanded γδ T-Cells.

Cancers·2026
Same author

Physical activity for public health in the 21st century.

Nature medicine·2026
Same author

Chronic exercise training intensity, immune cells, and cancer outcomes: a scoping review.

JNCI cancer spectrum·2026

Related Experiment Video

Updated: May 23, 2026

A Protein Suspension-Trapping Sample Preparation for Tear Proteomics by Liquid Chromatography-Tandem Mass Spectrometry
08:20

A Protein Suspension-Trapping Sample Preparation for Tear Proteomics by Liquid Chromatography-Tandem Mass Spectrometry

Published on: December 1, 2023

Fragmentation of protein using trypsin.

Richard J Simpson

    CSH Protocols
    |April 10, 2012
    PubMed
    Summary
    This summary is machine-generated.

    This protocol details using the protease trypsin for complete protein hydrolysis. High trypsin levels and denaturing conditions ensure total proteolysis, crucial for protein analysis.

    More Related Videos

    A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis
    09:40

    A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis

    Published on: April 28, 2022

    Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
    08:07

    Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

    Published on: July 26, 2019

    Related Experiment Videos

    Last Updated: May 23, 2026

    A Protein Suspension-Trapping Sample Preparation for Tear Proteomics by Liquid Chromatography-Tandem Mass Spectrometry
    08:20

    A Protein Suspension-Trapping Sample Preparation for Tear Proteomics by Liquid Chromatography-Tandem Mass Spectrometry

    Published on: December 1, 2023

    A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis
    09:40

    A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis

    Published on: April 28, 2022

    Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
    08:07

    Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

    Published on: July 26, 2019

    Area of Science:

    • Biochemistry
    • Proteomics

    Background:

    • Proteolysis is essential for protein analysis and characterization.
    • Trypsin is a widely used serine protease for protein digestion due to its specificity.

    Purpose of the Study:

    • To provide a protocol for complete protein hydrolysis using trypsin.
    • To outline conditions ensuring efficient and total proteolysis.

    Main Methods:

    • Utilizing high concentrations of the protease trypsin.
    • Performing proteolysis under denaturing conditions (e.g., guanidine-HCl, SDS, acetonitrile).
    • Employing chemical modifications like succinylation or citraconylation to limit cleavage sites.

    Main Results:

    • Achieved complete protein hydrolysis through optimized trypsin digestion.
    • Demonstrated successful proteolysis even under harsh denaturing conditions.
    • Showcased methods to control trypsin cleavage specificity.

    Conclusions:

    • The protocol ensures total protein digestion by trypsin.
    • Robustness of trypsin allows for effective proteolysis in denaturing environments.
    • Methods for site-specific cleavage enhance the utility of trypsin digestion.