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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.9K
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....
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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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...
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Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Histone Modification02:32

Histone Modification

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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...
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Updated: Mar 24, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
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Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

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Chemical Methods for Encoding and Decoding of Posttranslational Modifications.

Kelly N Chuh1, Anna R Batt1, Matthew R Pratt2

  • 1Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.

Cell Chemical Biology
|March 3, 2016
PubMed
Summary
This summary is machine-generated.

Chemical methods are crucial for studying protein posttranslational modifications, enabling the preparation and identification of modified proteins. These strategies are essential for advancing research in this complex and expanding field.

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Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Proteomics

Background:

  • Posttranslational modifications (PTMs) significantly alter protein properties and biological functions.
  • Traditional methods face challenges in site-specific analysis, comprehensive proteome profiling, and novel PTM detection.

Purpose of the Study:

  • To review the significant contributions of chemistry-based approaches to PTM research.
  • To highlight how chemical strategies aid in preparing modified proteins and characterizing PTMs in complex biological systems.

Main Methods:

  • Review of literature focusing on chemistry-based strategies for PTM analysis.
  • Examples of PTMs where chemical methods have been instrumental.

Main Results:

  • Chemical methods enable the preparation of homogeneously modified proteins.
  • These approaches facilitate the identification and characterization of PTMs within complex biological contexts.
  • Significant advancements have been made in understanding PTMs through chemical strategies.

Conclusions:

  • Chemistry-based approaches are vital for overcoming limitations in traditional PTM analysis.
  • As PTM diversity grows, chemical strategies will be indispensable for future research.
  • These methods are key to advancing the understanding of protein function and regulation.