Tandem mass spectrometry defines the stoichiometry and quaternary structural arrangement of tryptophan molecules in the multiprotein complex TRAP.

McCammon, MG; Hernández, H; Sobott, F; Robinson, CV

Abstract:

We have used tandem mass spectrometry to examine the stoichiometry and binding sites of trp molecules in various assemblies of the protein complex TRAP. The results show that TRAP forms oligomers containing 11 and 12 subunits. MS/MS experiments show that up to 11 trp molecules bind to the 12-mer but that during gas-phase dissociation 5 then 6 trp molecules are released reflecting the different gas-phase stabilities of the partially ligated forms. At high trp concentrations, the protein assemb...

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APA Style

McCammon, M. G., Hernández, H., Sobott, F., & Robinson, C. V. (2004). Tandem mass spectrometry defines the stoichiometry and quaternary structural arrangement of tryptophan molecules in the multiprotein complex TRAP. Journal of the American Chemical Society, 126(19), 5950–5951.

MLA Style

McCammon, M. G., et al. “Tandem Mass Spectrometry Defines the Stoichiometry and Quaternary Structural Arrangement of Tryptophan Molecules in the Multiprotein Complex TRAP.” Journal of the American Chemical Society, vol. 126, no. 19, Journal of the American Chemical Society, 2004, pp. 5950–51.

Chicago Style

McCammon, MG, H Hernández, F Sobott, and CV Robinson. 2004. “Tandem Mass Spectrometry Defines the Stoichiometry and Quaternary Structural Arrangement of Tryptophan Molecules in the Multiprotein Complex TRAP.” Journal of the American Chemical Society 126 (19): 5950–51.
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