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Published Online November 17, 2005
Science DOI: 10.1126/science.1120177

Reports

Submitted on September 14, 2005
Accepted on October 31, 2005

Evidence for Macromolecular Protein Rings in the Absence of Bulk Water

Brandon T. Ruotolo 1, Kevin Giles 2, Iain Campuzano 2, Alan M. Sandercock 1, Robert H. Bateman 2, Carol V. Robinson 1*

1 Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.
2 Waters MS Technologies Centre, Manchester, United Kingdom.

* To whom correspondence should be addressed.
Carol V. Robinson , E-mail: cvr24{at}cam.ac.uk

We have examined the architecture of a protein complex in the absence of bulk water. By determining collision cross-sections of assemblies of the trp RNA binding protein, TRAP, we discover that the 11-membered ring topology of the complex can be maintained within a mass spectrometer. We also find that the binding of tryptophan enhances the stability of the ring structure while addition of a specific RNA molecule increases the size of the complex and prevents structural collapse. These results provide definitive evidence that protein quaternary structure can be maintained in the absence of bulk water, and highlight the potential of ion mobility separation for defining shapes of heterogeneous macromolecular assemblies.


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