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Originally published in Science Express on 17 November 2005
Science 9 December 2005:
Vol. 310. no. 5754, pp. 1658 - 1661
DOI: 10.1126/science.1120177
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Reports

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. Robinson1*

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 established that the 11-membered ring topology of the complex can be maintained within a mass spectrometer. We also found that the binding of tryptophan enhances the stability of the ring structure and that 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.

1 Department of Chemistry, Lensfield Road, University of Cambridge, Cambridge CB2 1EW, UK.
2 Waters MS Technologies Centre, Manchester M55 5PP, UK.

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

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