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Related Concept Videos

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 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.
Protein Glycosylation01:25

Protein Glycosylation

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...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

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Related Experiment Video

Updated: Jul 15, 2026

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
08:12

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

Published on: January 8, 2018

Surface accessibility of protein post-translational modifications.

Chi Nam Ignatius Pang1, Andrew Hayen, Marc Ronald Wilkins

  • 1Systems Biology Group, School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW, Australia.

Journal of Proteome Research
|April 13, 2007
PubMed
Summary

Post-translational modifications (PTMs) influence protein function. This study reveals that PTMs involved in protein interactions are surface-associated, while others reside in the protein core or are artifacts.

More Related Videos

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

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

Published on: February 27, 2020

Related Experiment Videos

Last Updated: Jul 15, 2026

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins
08:12

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

Published on: January 8, 2018

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

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

Published on: February 27, 2020

Area of Science:

  • Biochemistry
  • Structural Biology
  • Proteomics

Background:

  • Protein post-translational modifications (PTMs) are essential for regulating protein function and cellular processes.
  • Understanding the structural context of PTMs is key to deciphering their functional roles.
  • Previous studies have highlighted the importance of PTMs, but their precise localization within protein structures remains an active area of research.

Purpose of the Study:

  • To investigate the structural environment of a large number of diverse post-translational modifications.
  • To determine the spatial distribution of different types of PTMs within protein structures.
  • To correlate PTM localization with their potential involvement in protein-protein interactions.

Main Methods:

  • Analysis of 8,378 incidences of 44 distinct post-translational modifications.
  • Utilized 19 different computational and structural analysis approaches.
  • Assessed the surface accessibility and core localization of modified amino acid residues.

Main Results:

  • PTMs implicated in protein-protein interactions, such as ester-linked phosphorylation, methylarginine, acetyllysine, sulfotyrosine, hydroxyproline, and hydroxylysine, were found to be predominantly surface-associated.
  • Other PTMs, including O-GlcNAc, phosphohistidine, 4-aspartylphosphate, methyllysine, and ADP-ribosylarginine, were located in the protein core or were not surface-associated.
  • Artifactual modifications exhibited random distribution throughout protein structures.

Conclusions:

  • The surface accessibility of specific post-translational modifications is a significant factor in mediating protein-protein interactions.
  • PTM localization provides insights into their functional roles, distinguishing interaction-mediating modifications from those in the protein core.
  • This study provides a comprehensive structural map of PTMs, enhancing our understanding of protein regulation and function.