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Rapid advances in structural genomics and in large-scale proteomic projects have yielded vast amounts of data on soluble proteins and their complexes. Despite these advances, progress in studying membrane proteins using mass spectrometry (MS) has been slow. This is due in part to the inherent solubility and dynamic properties of these proteins, but also to their low abundance and the absence of polar side chains in amino acid residues. Considerable progress in overcoming these challenges is, however, now being made for all levels of structural characterization. This progress includes MS studies of the primary structure of membrane proteins, wherein sophisticated enrichment and trapping procedures are allowing multiple posttranslational modifications to be defined through to the secondary structure level in which proteins and peptides have been probed using hydrogen exchange, covalent, or radiolytic labeling methods. Exciting possibilities now exist to go beyond primary and secondary structure to reveal the tertiary and quaternary interactions of soluble and membrane subunits within intact assemblies of more than 700 kDa.

Original publication

DOI

10.1146/annurev-biochem-062309-093307

Type

Journal article

Journal

Annu Rev Biochem

Publication Date

2011

Volume

80

Pages

247 - 271

Keywords

Cell Membrane, Detergents, Lipids, Mass Spectrometry, Membrane Microdomains, Membrane Proteins, Micelles, Models, Molecular, Multiprotein Complexes, Protein Conformation, Protein Folding, Protein Processing, Post-Translational, Proteomics