Ambient ionisation mass spectrometry for in situ analysis of intact proteins

Abstract

The interest in proteins is fuelled by their fundamental role in the biological processes occurring in living cells, both under normal conditions and in disease states. A key advantage of the analysis of proteins in their intact form is that all information relating to primary structure and posttranslational modifications is retained. Moreover, by considering intact proteins, it is possible to probe their tertiary (and quaternary) structures and interactions. In this perspective special feature, Helen Cooper and colleagues describe surface analysis techniques most commonly used for the mass spectrometric analysis of intact proteins, with emphasis on liquid extraction-based techniques focusing on in situ intact (top-down) protein analysis from biological surfaces such as tissue sections, dried blood spots, and bacterial communities. They also provide a brief overview of the potential future developments. Helen J. Cooper is Professor of Mass Spectrometry at the University of Birmingham (Birmingham, United Kingdom). Her main research interests are centered on the development and application of mass spectrometry techniques for the characterisation of biomolecular structures.