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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Protein Transport to the Thylakoids01:22

Protein Transport to the Thylakoids

Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...

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Related Experiment Video

Updated: Jun 8, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Accessing posttranslationally modified proteins through thiol positioning.

K S Ajish Kumar1, Ashraf Brik

  • 1Department of Chemistry, Ben-Gurion University of the Negev, Beer Sheva, Israel.

Journal of Peptide Science : an Official Publication of the European Peptide Society
|September 24, 2010
PubMed
Summary
This summary is machine-generated.

Native chemical ligation (NCL) and desulfurization enable efficient synthesis of modified proteins. Recent advancements expand the application of these chemical ligation methods for creating complex protein structures.

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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Area of Science:

  • Chemical Biology
  • Synthetic Chemistry
  • Protein Chemistry

Background:

  • Native chemical ligation (NCL) has revolutionized peptide and protein synthesis.
  • Desulfurization reactions are crucial for removing thiol-containing auxiliary groups.
  • Post-translational modifications are vital for protein function and regulation.

Purpose of the Study:

  • To review recent developments in chemical ligation strategies for protein synthesis.
  • To highlight the exploitation of ligation methods in creating post-translationally modified proteins.
  • To discuss advancements in desulfurization techniques for generating unmodified proteins.

Main Methods:

  • Utilizing native chemical ligation (NCL) for peptide bond formation.
  • Employing desulfurization reactions to remove auxiliary thiol groups.
  • Synthesizing proteins with various post-translational modifications.

Main Results:

  • Demonstrated the efficacy of NCL coupled with desulfurization for protein synthesis.
  • Showcased new ligation strategies enabling broader applications.
  • Successfully synthesized various post-translationally modified proteins.

Conclusions:

  • Chemical ligation methods, particularly NCL with desulfurization, are powerful tools for protein synthesis.
  • Ongoing research continues to evolve and expand the capabilities of ligation strategies.
  • These advancements facilitate the study of complex, modified proteins.