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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.
Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
Amines to Amides: Acylation of Amines01:19

Amines to Amides: Acylation of Amines

Various carboxylic acid derivatives (such as acid chlorides, esters, and anhydrides) can be used for the acylation of amines to yield amides. The reaction requires two equivalents of amines. The first amine molecule functions as a nucleophile and attacks the carbonyl carbon to produce a tetrahedral intermediate. This is followed by the loss of the leaving group and restoration of the C=O bond.
Next, the second equivalent of amine serves as a Brønsted base and deprotonates the quaternary amide...
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...

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Related Experiment Video

Updated: Jun 25, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
08:31

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

Published on: April 10, 2020

Analysis of protein acylation.

Ruth Zeidman1, Caroline S Jackson, Anthony I Magee

  • 1Molecular Medicine, National Heart & Lung Institute, Imperial College London, London, United Kingdom.

Current Protocols in Protein Science
|February 24, 2009
PubMed
Summary

This study details methods for analyzing protein acylation, including fatty acid identification and bond types. It covers metabolic labeling, bond cleavage sensitivity, and thin-layer chromatography for comprehensive protein acylation analysis.

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Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry
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Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry

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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Related Experiment Videos

Last Updated: Jun 25, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
08:31

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

Published on: April 10, 2020

Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry
07:27

Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry

Published on: April 9, 2021

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
12:49

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein acylation, the attachment of fatty acids to proteins, significantly impacts protein function and localization.
  • Various fatty acids can acylate proteins through distinct covalent bonds, necessitating specific analytical approaches.

Purpose of the Study:

  • To describe comprehensive methods for analyzing protein acylation.
  • To enable the identification of specific fatty acids and covalent bonds involved in protein acylation.
  • To quantify the levels of protein acylation.

Main Methods:

  • Metabolic labeling of proteins using tritiated fatty acids.
  • Differential chemical cleavage to distinguish between various types of covalent bonds.
  • Thin-layer chromatography for the separation and identification of protein-associated fatty acids.

Main Results:

  • Established protocols for analyzing protein acylation levels.
  • Developed methods for identifying the specific fatty acid and bond type in acylated proteins.
  • Demonstrated the utility of metabolic labeling and chromatographic techniques.

Conclusions:

  • The described methods provide a robust framework for the detailed analysis of protein acylation.
  • Accurate characterization of protein acylation is crucial for understanding protein function and regulation.
  • These techniques facilitate research into the diverse roles of protein acylation in cellular processes.