Abstract
Protein synthesis and its folding to form quaternary structures are generally not sufficient to produce a functional protein. Proteins, soon after their translation, are often modified to achieve proper folding and localization. Some of the post-translational modifications include proteolytic cleavage, addition of prosthetic groups and addition of functional groups like phosphoryl, acetyl or methyl groups, the latter being reversible, and constitute an important role in modulating the activity of the protein. Post-translational modifications of proteins also regulate their stability as well as interactions with other proteins and macromolecules. Identification and understanding of the functions performed by the modified proteins is critical in the study of cellular homeostasis. It may provide new drug targets and also offer candidates for biomarker selection involved in chronic diseases. This chapter describes various post-translational modifications that occur in proteins and some of the key biological functions and signalling pathways controlled by these modifications in a living cell.
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Mittal, S., Saluja, D. (2015). Protein Post-translational Modifications: Role in Protein Structure, Function and Stability. In: Singh, L.R., Dar, T.A., Ahmad, P. (eds) Proteostasis and Chaperone Surveillance. Springer, New Delhi. https://doi.org/10.1007/978-81-322-2467-9_2
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DOI: https://doi.org/10.1007/978-81-322-2467-9_2
Publisher Name: Springer, New Delhi
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