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Discuss Post-translational modification of proteins and provide two examples of modifications and describe it. (short answer)

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Protein post-translational modifications (PTMs) increase the proteome's functional diversity by the covalent addition of functional
groups or proteins, proteolytic cleavage of regulatory subunits, or degradation of complete proteins. Examples of this modification
include phosphorylation, glycosylation, ubiquitination, nitrosylation, methylation, acetylation, lipidation, and proteolysis and influence
almost all typical cell biology aspects pathogenesis. Hence, identifying and understanding PTMs is critical in studying cell biology and
disease treatment and prevention.
 Step-by-step explanation

Generally, proteins are synthesized by ribosomes translating mRNA into polypeptide chains, which may then undergo
PTM to form the mature protein product. PTMs are essential components in cell signaling, for example, when
prohormones are converted to hormones.
Post-translational modifications can occur on the amino acid side chains or at the protein's C- or N- termini.
They can extend the 20 standard amino acids' chemical repertoire by modifying an existing functional group or
introducing a new one such as phosphate. Phosphorylation is an often mechanism for regulating the activity of enzymes
and is the most common post-translational modification.
Many eukaryotic and prokaryotic proteins also have carbohydrate molecules attached to them in a process called
glycosylation, which can promote protein folding and improve stability and serve regulatory functions. Attachment of lipid
molecules, known as lipidation, often targets a protein or part of a protein attached to the cell membrane.

Examples of Post-translational modification

Proteolytic cleavage is one of the common modifications where proteins are cleaved to remove some additional amino
acid(s) or protein portions. Examples are zymogens, which are inactive forms of enzymes and are activated by removing
some portion of the protein.
References
Walsh, C. (2006). Posttranslational modification of proteins: expanding nature's inventory. Roberts and Company
Publishers.

Rogers, L. D., & Overall, C. M. (2013). Proteolytic post-translational modification of proteins: proteomic tools and
methodology. Molecular & Cellular Proteomics, 12(12), 3532-3542.

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