Toward a general chemical method for rapidly mapping multi-protein complexes

Journal of Proteome Research
C Denison, Thomas Kodadek

Abstract

Ru(II)(bpy2)32+Cl2, ammonium persulfate, and visible light irradiation has been shown to rapidly and efficiently cross-link several interacting proteins. However, this methodology has not yet been used to map the architecture of large multi-protein complexes. In this study, this chemistry is applied to the crystallographically characterized yeast proteasome. The data obtained demonstrate both the method's increased generality and fidelity in comparison to traditional bifunctional cross-linking reagents, while also highlighting the future need for developing better analytical techniques to separate cross-linked products.

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Citations

Jan 31, 2006·Journal of the American Society for Mass Spectrometry·Sara P GaucherMalin M Young
Apr 6, 2005·Trends in Pharmacological Sciences·Thomas KodadekJean-Claude Bonnafous
Nov 23, 2006·Journal of the American Chemical Society·Bo LiuThomas Kodadek
Jun 3, 2008·The Journal of Biological Chemistry·Chase T ArcherThomas Kodadek
Feb 12, 2005·The Journal of Peptide Research : Official Journal of the American Peptide Society·H-J Lin, T Kodadek
Mar 21, 2013·Chemical Reviews·Christopher K PrierDavid W C MacMillan
Feb 12, 2013·Chemical Society Reviews·George W Preston, Andrew J Wilson
Jan 30, 2008·Current Protocols in Cell Biology·Karsten Melcher, Hung-Ta Chen
Sep 16, 2004·Journal of the American Chemical Society·Lyle BurdineThomas Kodadek

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