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

Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

7.8K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
7.8K
Global Climate Change01:50

Global Climate Change

29.0K
Throughout its ~4.5 billion year history, the Earth has experienced periods of warming and cooling. However, the current drastic increase in global temperatures is well outside of the Earth’s cyclic norms, and evidence for human-caused global climate change is compelling. Paleoclimatology, the study of ancient climate conditions, provides ample evidence for human-caused global climate change by comparing recent conditions with those in the past.
29.0K
Translation01:31

Translation

157.3K
Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of...
157.3K
Translation01:31

Translation

18.0K
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Proteins are...
18.0K
Histone Modification02:32

Histone Modification

16.3K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
16.3K
Initiation of Translation02:33

Initiation of Translation

39.2K
Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
39.2K

You might also read

Related Articles

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

Sort by
Same author

Rapid Peptide Mapping of Monoclonal Antibodies with Direct Infusion Mass Spectrometry.

bioRxiv : the preprint server for biology·2026
Same author

Directed evolution of APOX for proximity labeling using phenols with high redox potentials.

Cell chemical biology·2026
Same author

Interactome screening implicates BAG6 as a suppressor of UBQLN2 misfolding in ALS/FTD.

Frontiers in molecular neuroscience·2026
Same author

DNA-damage dependent isoform switching modulates RIF1 DNA repair complex assembly and phase separation.

The Journal of biological chemistry·2026
Same author

Interactome screening implicates BAG6 as a suppressor of UBQLN2 misfolding in ALS-dementia.

bioRxiv : the preprint server for biology·2025
Same author

A needed nomenclature for nucleosomes.

Molecular cell·2025

Related Experiment Video

Updated: Feb 12, 2026

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

4.5K

Enhanced Global Post-translational Modification Discovery with MetaMorpheus.

Stefan K Solntsev, Michael R Shortreed, Brian L Frey

    Journal of Proteome Research
    |March 27, 2018
    PubMed
    Summary

    Enhanced G-PTM-D with multinotch searches improves protein post-translational modification (PTM) identification accuracy and speed. This advanced technique increases identified modifications by 20% and significantly reduces search time.

    Keywords:
    G-PTM-Dcalibrationcoisolationdatabase searchpost-translational modificationpost-translational modification discoveryproteomics

    More Related Videos

    Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications
    10:12

    Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications

    Published on: April 21, 2023

    3.7K
    Identification of Post-translational Modifications of Plant Protein Complexes
    10:07

    Identification of Post-translational Modifications of Plant Protein Complexes

    Published on: February 22, 2014

    24.6K

    Related Experiment Videos

    Last Updated: Feb 12, 2026

    Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
    08:12

    Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

    Published on: May 5, 2022

    4.5K
    Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications
    10:12

    Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications

    Published on: April 21, 2023

    3.7K
    Identification of Post-translational Modifications of Plant Protein Complexes
    10:07

    Identification of Post-translational Modifications of Plant Protein Complexes

    Published on: February 22, 2014

    24.6K

    Area of Science:

    • Proteomics
    • Biochemistry
    • Computational Biology

    Background:

    • Accurate identification of protein post-translational modifications (PTMs) is essential for understanding protein function and biological processes.
    • Global PTM identification and localization techniques are critical for comprehensive proteome analysis.
    • Existing methods may face limitations in accuracy, speed, and scope, particularly for complex modifications.

    Purpose of the Study:

    • To enhance the G-PTM-D technique for more accurate and efficient global identification and localization of protein post-translational modifications.
    • To demonstrate the effectiveness of multinotch searches in improving PTM identification, including high-mass modifications like glycosylations.
    • To integrate spectral calibration and algorithmic enhancements into a comprehensive workflow for PTM analysis.

    Main Methods:

    • Applied spectral file calibration prior to the G-PTM-D analysis.
    • Incorporated algorithmic enhancements into the peptide database search.
    • Utilized multinotch searches to augment the G-PTM-D workflow for PTM identification.
    • Integrated the complete workflow into the MetaMorpheus software tool.

    Main Results:

    • Achieved a 20% increase in the number of identified protein post-translational modifications.
    • Reduced the PTM identification search time by an order of magnitude.
    • Successfully identified numerous PTM types, including challenging high-mass modifications such as glycosylations.
    • Demonstrated the utility of multinotch searches beyond G-PTM-D, outperforming standard database search methods.

    Conclusions:

    • The enhanced G-PTM-D workflow, incorporating spectral calibration and multinotch searches, significantly improves the accuracy, speed, and scope of PTM identification.
    • MetaMorpheus provides a comprehensive software solution for advanced PTM analysis.
    • Multinotch searches represent a broadly applicable advancement for peptide database searching in proteomics.