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Nucleic Acids Research Advance Access originally published online on February 7, 2007
Nucleic Acids Research 2007 35(6):e39; doi:10.1093/nar/gkm030
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Nucleic Acids Research, 2007, Vol. 35, No. 6 e39
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Methods Online

Rapid coupling of Surface Plasmon Resonance (SPR and SPRi) and ProteinChipTM based mass spectrometry for the identification of proteins in nucleoprotein interactions

Emeline Bouffartigues1, Hervé Leh1, Marielle Anger-Leroy2, Sylvie Rimsky1 and Malcolm Buckle1,*

1Enzymologie et cinétique structurale, Laboratoire de Biotechnologies et de Pharmacologie génétique Appliquée, UMR 8113 CNRS, Institut d’Alembert, Ecole Normale Supérieur de Cachan. 61 Ave. du Président Wilson F-94235 Cachan and 2GenOptics SA Centre Scientifique, Plateau du Moulon, Bâtiment 503, F-91403 Orsay, France

*To whom correspondence should be addressed. Tel: +33-147407673; Fax: +33-147407684; Email: buckle{at}lbpa.ens-cachan.fr

Received July 7, 2006. Revised January 3, 2007. Accepted January 5, 2007.

We compared coupling approaches of SPR to LC-MS and ProteinChipTM-based mass spectrometry (SELDITM) as a means of identifying proteins captured on DNA surfaces. The approach we outline has the potential to allow multiple, quantitative analysis of macromolecular interactions followed by rapid mass spectrometry identification of retained material.


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