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Covalently Linked Protein Regulators

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 RER

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 Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Related Experiment Video

Updated: Jul 18, 2026

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

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

Published on: February 27, 2020

A point-process model for rapid identification of post-translational modifications.

Bo Yan¹, Tong Zhou, Peng Wang

¹Department of Biochemical and Molecular Biology, University of Georgia, GA, USA.

Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing

|November 11, 2006

Summary

This study introduces a novel point-process model for rapid, high-throughput detection of post-translational modifications (PTMs). The new method efficiently identifies all PTM types in mass spectrometry data without prior knowledge, improving upon existing techniques.

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

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

Published on: May 22, 2018

Related Experiment Videos

Last Updated: Jul 18, 2026

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

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

Published on: February 27, 2020

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

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:

Biochemistry
Proteomics
Computational Biology

Background:

Post-translational modifications (PTMs) are crucial for biological functions but challenging to detect and identify, especially at high throughput.
Current methods often involve time-consuming exhaustive searches, limiting the scope of PTM analysis.

Purpose of the Study:

To develop a rapid and efficient computational method for identifying all types of post-translational modifications (PTMs) in mass spectrometry data.
To enable blind PTM searches without pre-specifying modification types.

Main Methods:

A point-process model was developed to optimize mass shifts for maximizing spectral alignment between experimental and theoretical MS/MS spectra.
Cross-correlation calculations were employed to achieve rapid searching across all PTM types.
The approach facilitates blind identification of PTMs, requiring no prior knowledge of modification types.

Main Results:

The new point-process model demonstrated comparable or superior performance to existing blind search methods.
The approach offers significant computational efficiency and conceptual simplicity.
It enables high-throughput identification of diverse PTMs.

Conclusions:

The developed point-process model provides a more efficient and simpler solution for comprehensive PTM detection in proteomics.
This method advances high-throughput analysis of PTMs, crucial for understanding biological functions.
The blind search capability broadens the applicability of mass spectrometry in PTM discovery.