Identification of Posttranslational Modifications (PTMs) of Proteins by  Mass Spectrometry.

Identification of Posttranslational Modifications (PTMs) of Proteins by Mass Spectrometry. Adv Exp Med Biol. 2019;1140:199-224 Authors: Aslebagh R, Wormwood KL, Channaveerappa D, Wetie AGN, Woods AG, Darie CC Abstract There are only 30,000 human genes, which, according to the central dogma from biology, it means that there should be 30,000 mRNA and 30,000 proteins. However, there are at least 1-2 million protein entities that are expressed in a cell at a given time. This is primarily due to alternative splicing in different cells and tissues, which may lead to expression of different protein isoforms within one cell, but also different protein isoforms in different tissues. A new level of complexity of proteins and protein isoforms is then given by posttranslational modifications (PTMs) of proteins. Here, we discuss the PTMs in proteins and how they are identified by mass spectrometry and proteomics, with specific examples on identification of acetylation, phosphorylation, glycosylation, alkylation, hydroxinonenal-modification or assignment of intramolecular and intermolecular disulfide bridges. PMID: 31347049 [PubMed - in process]
Source: Advances in Experimental Medicine and Biology - Category: Research Tags: Adv Exp Med Biol Source Type: research