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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.

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.

Oxidations of Aldehydes and Ketones to Carboxylic Acids

Oxidations of Aldehydes and Ketones to Carboxylic Acids

Oxidation of aldehydes and ketones results in the formation of carboxylic acids. Aldehydes, bearing hydrogen next to the carbonyl group, are easily oxidized compared to ketones. This is because an aldehydic proton can easily be abstracted during oxidation.
Aldehydes readily undergo oxidation in strong oxidizing agents such as potassium permanganate and chromic acid. The oxidation can also be carried out using mild oxidizing agents such as silver oxide. In fact, aldehydes can be easily oxidized...

Radical Autoxidation

Radical Autoxidation

The oxidation of an organic compound in the presence of air or oxygen is called autoxidation. For example, cumene reacts with oxygen to form hydroperoxide. Autoxidation involves initiation, propagation, and termination steps. Many organic compounds are susceptible to autoxidation—especially ethers in the presence of oxygen, which form hydroperoxides. Even though this reaction is slow, old ether bottles contain small amounts of peroxide, which leads to laboratory explosions during ether...

Oxidation of Alcohols

Oxidation of Alcohols

In this lesson, the oxidation of alcohols is discussed in depth. The various reagents used for oxidation of primary and secondary alcohols are detailed, and their mechanism of action is provided.
The process of oxidation in a chemical reaction is observed in any of the three forms:

Oxidation of Phenols to Quinones

Oxidation of Phenols to Quinones

In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox property is crucial in...

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Related Experiment Video

Updated: Jun 23, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

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Quantification of protein modification by oxidants.

Clare L Hawkins¹, Philip E Morgan, Michael J Davies

¹The Heart Research Institute, Camperdown, NSW, Australia.

Free Radical Biology & Medicine

|May 15, 2009

Summary

Proteins readily undergo oxidative damage from reactive species, leading to amino acid changes. This review evaluates methods for quantifying protein damage, focusing on absolute quantification techniques.

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Area of Science:

Biochemistry
Oxidative Stress Research

Background:

Proteins are susceptible to oxidative damage due to their high abundance and reactivity with radicals and excited states like singlet oxygen.
Oxidant exposure causes amino acid modification, intermediate formation, and stable product generation, all indicators of protein damage.

Purpose of the Study:

To review and discuss various methods for quantifying protein oxidative damage.
To emphasize techniques providing absolute quantitative data on protein modification extent.
To provide detailed method sheets for commonly used techniques.

Main Methods:

Review of existing literature on protein oxidation quantification.
Comparative analysis of different quantification approaches.
Inclusion of detailed protocols for selected methods.

Main Results:

Discussion of the advantages and disadvantages of various protein damage quantification methods.
Identification of methods suitable for absolute quantification of protein modification.
Provision of practical guidance through detailed method sheets.

Conclusions:

Accurate quantification of protein oxidative damage is crucial for understanding biological processes.
Methods yielding absolute quantitative data are preferred for precise assessment of protein modification.
This review serves as a comprehensive resource for researchers studying protein oxidation.