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Cell Syst. 2018 Jan 24;6(1):136-141.e5. doi: 10.1016/j.cels.2017.10.017. Epub 2017 Nov 29.

Chemical Crosslinking Mass Spectrometry Analysis of Protein Conformations and Supercomplexes in Heart Tissue.

Author information

1
Department of Genome Sciences, University of Washington, Seattle, WA 98105, USA.
2
Department of Bioengineering, University of Washington, Seattle, WA 98105, USA; Department of Anesthesiology and Pain Medicine, University of Washington, Seattle, WA 98105, USA; Mitochondria and Metabolism Center, University of Washington, Seattle, WA 98105, USA.
3
Department of Genome Sciences, University of Washington, Seattle, WA 98105, USA. Electronic address: jimbruce@uw.edu.

Abstract

While modern structural biology technologies have greatly expanded the size and type of protein complexes that can now be studied, the ability to derive large-scale structural information on proteins and complexes as they exist within tissues is practically nonexistent. Here, we demonstrate the application of crosslinking mass spectrometry to identify protein structural features and interactions in tissue samples, providing systems structural biology insight into protein complexes as they exist in the mouse heart. This includes insights into multiple conformational states of sarcomere proteins, as well as interactions among OXPHOS complexes indicative of supercomplex assembly. The extension of crosslinking mass spectrometry analysis into the realm of tissues opens the door to increasing our understanding of protein structures and interactions within the context of the greater biological system.

KEYWORDS:

crosslinking; heart tissue; interactome; mass spectrometry; mitochondria; protein interactions; respiration; sarcomere; supercomplex; systems structural biology

PMID:
29199018
PMCID:
PMC5799023
[Available on 2019-01-24]
DOI:
10.1016/j.cels.2017.10.017

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