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

Academic Article
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Overview

authors

  • Denison, C.
  • Kodadek, Thomas

publication date

  • May 2004

journal

  • Journal of Proteome Research  Journal

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.

subject areas

  • Cross-Linking Reagents
  • Mass Spectrometry
  • Models, Molecular
  • Multiprotein Complexes
  • Proteasome Endopeptidase Complex
  • Saccharomyces cerevisiae
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Research

keywords

  • PICUP
  • cross-linking
  • proteasome
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Identity

International Standard Serial Number (ISSN)

  • 1535-3893

Digital Object Identifier (DOI)

  • 10.1021/pr034071j

PubMed ID

  • 15253422
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Additional Document Info

start page

  • 417

end page

  • 425

volume

  • 3

issue

  • 3

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