Technical Note
Version 1
This version is not peer-reviewed
Proteomics and PTMomics to Unveil Metabolic Regulation
Version 1
: Received: 25 July 2024 / Approved: 25 July 2024 / Online: 26 July 2024 (08:24:57 CEST)
How to cite: Zhang, H. Proteomics and PTMomics to Unveil Metabolic Regulation. Preprints 2024, 2024072071. https://doi.org/10.20944/preprints202407.2071.v1 Zhang, H. Proteomics and PTMomics to Unveil Metabolic Regulation. Preprints 2024, 2024072071. https://doi.org/10.20944/preprints202407.2071.v1
Abstract
Proteomics is the study of cellular proteome by investigating how different proteins interact with each other and the roles they play in the organism. For mRNA expression levels do not always correlate well with protein expression levels, and the study of mRNA does not consider protein posttranslational modifications (PTMs), complex formation and localization; all of which are key to protein function. Quantitative proteomics uses mass spectrometry to identify and quantify proteins so as to find differentially expressed proteins under different condition. This allows us to gain biological insights under stress or other pathological conditions. posttranslational modifications, such as lysine acetylation, succinylation and lactylation, occur after protein biosynthesis and play vital roles in protein activity and cell physiology regulation. Here we present the mass spectrometry analysis in detail to unveil protein acylase and deacylase’ roles in metabolic regulation based on PTMomics lysine acetylome and suincylome.
Keywords
quantitative proteomics; mass spectrometry; post translational modifications (PTMs); acetylation; succinylation; lactylation
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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