Evidence for macromolecular protein rings in the absence of bulk water.

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 foun...

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Detalhes bibliográficos
Main Authors: Ruotolo, B, Giles, K, Campuzano, I, Sandercock, A, Bateman, R, Robinson, C
Formato: Journal article
Idioma:English
Publicado em: 2005
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author Ruotolo, B
Giles, K
Campuzano, I
Sandercock, A
Bateman, R
Robinson, C
author_facet Ruotolo, B
Giles, K
Campuzano, I
Sandercock, A
Bateman, R
Robinson, C
author_sort Ruotolo, B
collection OXFORD
description 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.
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spelling oxford-uuid:eb0701a4-802e-4ba9-90d0-1bce725dcad52022-03-27T11:06:34ZEvidence for macromolecular protein rings in the absence of bulk water.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:eb0701a4-802e-4ba9-90d0-1bce725dcad5EnglishSymplectic Elements at Oxford2005Ruotolo, BGiles, KCampuzano, ISandercock, ABateman, RRobinson, CWe 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.
spellingShingle Ruotolo, B
Giles, K
Campuzano, I
Sandercock, A
Bateman, R
Robinson, C
Evidence for macromolecular protein rings in the absence of bulk water.
title Evidence for macromolecular protein rings in the absence of bulk water.
title_full Evidence for macromolecular protein rings in the absence of bulk water.
title_fullStr Evidence for macromolecular protein rings in the absence of bulk water.
title_full_unstemmed Evidence for macromolecular protein rings in the absence of bulk water.
title_short Evidence for macromolecular protein rings in the absence of bulk water.
title_sort evidence for macromolecular protein rings in the absence of bulk water
work_keys_str_mv AT ruotolob evidenceformacromolecularproteinringsintheabsenceofbulkwater
AT gilesk evidenceformacromolecularproteinringsintheabsenceofbulkwater
AT campuzanoi evidenceformacromolecularproteinringsintheabsenceofbulkwater
AT sandercocka evidenceformacromolecularproteinringsintheabsenceofbulkwater
AT batemanr evidenceformacromolecularproteinringsintheabsenceofbulkwater
AT robinsonc evidenceformacromolecularproteinringsintheabsenceofbulkwater