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

Journal article

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 ...

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Authors: Ruotolo, B; Giles, K; Campuzano, I; Sandercock, A; Bateman, R

• Journal: Science
• Volume: 310
• Issue: 5754
• Pages: 1658-1661
• Place of publication: United States
• Publication date: 2005-12-09
• DOI: 10.1126/science.1120177
• EISSN: 1095-9203
• ISSN: 0036-8075
• Language: English
• Keywords: Water; RNA-Binding Proteins; Spectrometry, Mass, Electrospray Ionization; Transcription Factors; Apoproteins; Bacillus subtilis; Tryptophan; Protein Subunits; Protein Conformation; 5' Untranslated Regions; Bacterial Proteins; Thermodynamics; Protein Structure, Quaternary; Ions; Chemistry, Physical; Physicochemical Phenomena