Total Redox-Modified Proteome
Redox modifications are a crucial form of protein modification that occurs in living organisms. These modifications regulate the redox state of proteins, affecting their structure, function, and activity. Generally, redox modifications can be categorized into oxidative and reductive modifications.
Oxidative Modifications
1. Cysteine Oxidation
Cysteine is a prevalent target for oxidative modifications. It can be oxidized into various forms, including cysteic acid and cystine, among other derivatives.
2. Thiol Oxidation
The oxidation of thiol groups can cause alterations in the three-dimensional structure of proteins, thereby influencing their functional properties.
3. Methionine Oxidation
Under specific conditions, methionine can be oxidized, forming methionine sulfoxide and other oxidized products.
Reductive Modifications
1. Disulfide Bond Formation
Certain proteins require the formation of disulfide bonds to maintain structural stability and proper function.
2. Thiol Reduction
Reduction processes can revert oxidized thiols back to their active forms.
In summary, the total redox-modified proteome encompasses all proteins that have been subject to oxidative and reductive modifications. Investigating this subset of the proteome enhances our understanding of redox balance mechanisms in cells and reveals the impact of these modifications on biological functions and disease development.
MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.
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