Journal
NATURE CHEMISTRY
Volume 10, Issue 2, Pages 139-148Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEM.2908
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Funding
- US National Institutes of Health [R01 GM103479, S10 RR028893]
- US Department of Energy (UCLA/DOE Institute for Genomics and Proteomics) [DE-FC03-02ER63421]
- American Society for Mass Spectrometry
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Mass spectrometry (MS) has become a crucial technique for the analysis of protein complexes. Native MS has traditionally examined protein subunit arrangements, while proteomics MS has focused on sequence identification. These two techniques are usually performed separately without taking advantage of the synergies between them. Here we describe the development of an integrated native MS and top-down proteomics method using Fourier-transform ion cyclotron resonance (FTICR) to analyse macromolecular protein complexes in a single experiment. We address previous concerns of employing FTICR MS to measure large macromolecular complexes by demonstrating the detection of complexes up to 1.8 MDa, and we demonstrate the efficacy of this technique for direct acquirement of sequence to higher-order structural information with several large complexes. We then summarize the unique functionalities of different activation/dissociation techniques. The platform expands the ability of MS to integrate proteomics and structural biology to provide insights into protein structure, function and regulation.
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