Proteomics is the large-scale study of proteins.[1][2] Proteins are vital parts of living organisms, with many functions. The term proteomics was coined in 1997[3] in analogy with genomics, the study of the genome. The word proteome is a portmanteau of protein and genome, and was coined by Marc Wilkins in 1994 while he was a PhD student at Macquarie University.[4] Macquarie University also founded the first dedicated proteomics laboratory in 1995[5] (the Australian Proteome Analysis Facility – APAF).[6]

The proteome is the entire set of proteins that are produced or modified by an organism or system. This varies with time and distinct requirements, or stresses, that a cell or organism undergoes.[7] Proteomics is an interdisciplinary domain that has benefitted greatly from the genetic information of the Human Genome Project;[8] it also covers emerging scientific research and the exploration of proteomes from the overall level of intracellular protein composition, structure, and its own unique activity patterns. It is an important component of functional genomics.

Proteomics generally refers to the large-scale experimental analysis of proteins and is often specifically used to refer to protein purification and mass spectrometry.

After genomics and transcriptomics, proteomics is the next step in the study of biological systems. It is more complicated than genomics because an organism's genome is more or less constant, whereas the proteome differs from cell to cell and from time to time. Distinct genes are expressed in different cell types, which means that even the basic set of proteins that are produced in a cell needs to be identified.

In the past this phenomenon was done by RNA analysis, but it was found not to correlate with protein content.[9][10] It is now known that mRNA is not always translated into protein,[11] and the amount of protein produced for a given amount of mRNA depends on the gene it is transcribed from and on the current physiological state of the cell. Proteomics confirms the presence of the protein and provides a direct measure of the quantity present.

Not only does the translation from mRNA cause differences, but many proteins are also subjected to a wide variety of chemical modifications after translation. Many of these post-translational modifications are critical to the protein's function.

One such modification is phosphorylation, which happens to many enzymes and structural proteins in the process of cell signaling. The addition of a phosphate to particular amino acids—most commonly serine and threonine[12] mediated by serine/threonine kinases, or more rarely tyrosine mediated by tyrosine kinases—causes a protein to become a target for binding or interacting with a distinct set of other proteins that recognize the phosphorylated domain.

Because protein phosphorylation is one of the most-studied protein modifications, many "proteomic" efforts are geared to determining the set of phosphorylated proteins in a particular cell or tissue-type under particular circumstances. This alerts the scientist to the signaling pathways that may be active in that instance.

This page was last edited on 26 June 2018, at 00:21 (UTC).
Reference: under CC BY-SA license.

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