PROTEINS 2015* A native mass spectrometry view at Complement activation and CRISP-Cas systems (#19)
Around for more than a century the analytical technique of mass spectrometry is blooming more than ever, and applied in nearly all aspects of the natural and life sciences. In the last two decades mass spectrometry has become routine for the high-throughput analysis of peptides. However, also intact proteins and even complete protein complexes can nowadays be analyzed, enabling MS to contribute also to the field of structural biology. In this lecture, I will describe the emerging role of mass spectrometry with its different technical facets in structural biology, focusing especially on the analysis of dynamic protein assemblies.
In this talk I will focus on the structural elucidation of CRISPR-Cas complexes from different bacterial origins, highlighting the interplay in between mass spectrometry, molecular biology and electron microscopy1. The unique features of native MS will be further highlighted in a study on the initial step of Complement activation, whereby native mass spectrometry was used to reveal the unique role of IgG hexamers in the initial activation2. I will also describe how native mass spectrometry can also be used to study kinase-substrate relationships, monitoring not only protein phosphorylation quantitatively, but also how this effects protein structure and association with other proteins3.
