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MEMBRANE PROTEOME FOR ANALYSIS BY LATER MASS SPECTROMETRY

Mohammad Fatemeh

Proteins, glycolipids, and phospholipids make up cellular membranes, which are crucial for protecting and limiting metabolic processes within cells while also preserving cellular integrity and homeostasis. Membrane proteins serve as receptors, transporters, adhesion-anchors, enzymes, and many other crucial tasks. The determination of the plasma membrane (PM) proteome, resolution of membrane protein topology, establishment of numerous receptor protein complexes, identification of ligand-receptor pairs, and elucidation of signalling networks originating at the PM have all benefited from recent developments in proteomic mass spectrometry. Here, we discuss the remarkable acceleration of the development of a full membrane proteome by discovery-based proteomic algorithms. Most membrane proteins are less abundant and more hydrophobic than typical soluble proteins, which makes study of these proteins more challenging. The sample preparation, which includes the enrichment and dissolution of the membrane proteins, is crucial for the successful identification of membrane proteins. The enrichment of low-abundance membrane proteins at membrane and/or protein levels and the dissolution of hydrophobic membrane proteins have both been accomplished using a variety of established and recently developed techniques.