Mass Spectrometric (MS) Analysis of Proteins and Peptides

Author:

Jayathirtha Madhuri1,Dupree Emmalyn J.1,Manzoor Zaen1,Larose Brianna1,Sechrist Zach1,Neagu Anca-Narcisa2,Petre Brindusa Alina3,Darie Costel C.1ORCID

Affiliation:

1. Biochemistry & Proteomics Group, Department of Chemistry and Biomolecular Science, Clarkson University, 8 Clarkson Avenue, Potsdam, NY, United States

2. Laboratory of Animal Histology, Faculty of Biology, “Alexandru Ioan Cuza” University of Iasi, Iasi, Romania

3. Laboratory of Biochemistry, Department of Chemistry, Al. I. Cuza University of Iasi, Iasi, Romania, Center for Fundamental Research and Experimental Development in Translation Medicine – TRANSCEND, Regional Institute of Oncology, Iasi, Romania

Abstract

: The human genome is sequenced and comprised of ~30,000 genes, making humans just a little bit more complicated than worms or flies. However, complexity of humans is given by proteins that these genes code for because one gene can produce many proteins mostly through alternative splicing and tissue-dependent expression of particular proteins. In addition, post-translational modifications (PTMs) in proteins greatly increase the number of gene products or protein isoforms. Furthermore, stable and transient interactions between proteins, protein isoforms/proteoforms and PTM-ed proteins (protein-protein interactions, PPI) add yet another level of complexity in humans and other organisms. In the past, all of these proteins were analyzed one at the time. Currently, they are analyzed by a less tedious method: mass spectrometry (MS) for two reasons: 1) because of the complexity of proteins, protein PTMs and PPIs and 2) because MS is the only method that can keep up with such a complex array of features. Here, we discuss the applications of mass spectrometry in protein analysis..

Publisher

Bentham Science Publishers Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry,General Medicine

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