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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.
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.
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
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...
Protecting Groups for Aldehydes and Ketones: Introduction01:23

Protecting Groups for Aldehydes and Ketones: Introduction

Protecting groups are compounds that can bind to a specific functional group in the presence of other functional groups to protect them from undesired chemical reactions. These compounds can selectively bind to particular functional groups and advance chemoselective reactions in polyfunctional systems (Figure 1). After the functional group has served its purpose, it is removed by reacting it with specific compounds.
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Related Experiment Video

Updated: Jun 19, 2026

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations
05:57

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Published on: April 26, 2024

Rules governing selective protein carbonylation.

Etienne Maisonneuve1, Adrien Ducret, Pierre Khoueiry

  • 1Laboratoire de Chimie Bactérienne - Aix Marseille Université - UPR 9043-CNRS, 31, Chemin Joseph Aiguier, Marseille, France.

Plos One
|October 6, 2009
PubMed
Summary
This summary is machine-generated.

Researchers developed a predictive model to identify proteins prone to metal-catalyzed oxidation (MCO). This model accurately predicts carbonylated sites and proteins, aiding in understanding protein carbonylation across organisms.

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Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations
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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
  • Proteomics
  • Bioinformatics

Background:

  • Carbonyl derivatives form via metal-catalyzed oxidation (MCO) targeting specific amino acid residues.
  • The susceptibility of proteins to carbonylation is not fully understood, with only certain proteins being prone to this modification.

Purpose of the Study:

  • To identify and characterize carbonylated sites in proteins.
  • To develop predictive rules for identifying carbonylation-prone sites.
  • To create an in silico model for predicting protein carbonylation.

Main Methods:

  • Mass spectrometry was employed to identify carbonylated sites in bovine serum albumin (BSA) and Escherichia coli proteins.
  • Analysis of carbonylated sites revealed 'hot spots' and neighboring site susceptibility.
  • An in silico model was developed based on identified rules for predicting carbonylation-prone sites.

Main Results:

  • Identified specific carbonylated sites in BSA and 23 proteins from E. coli.
  • Established that adjacent sites become more susceptible to carbonylation once a site is modified.
  • Developed a predictive model (http://www.lcb.cnrs-mrs.fr/CSPD/) for accurate prediction of carbonylation sites and prone proteins in E. coli.

Conclusions:

  • Proteins evolve to either retain or lose predicted carbonylation 'hot spots' based on their biological roles.
  • The predictive model demonstrates efficacy in detecting carbonylated proteins in Bacillus subtilis.
  • The developed model holds potential for extension to study MCO attacks across diverse organisms.