Open Access. Powered by Scholars. Published by Universities.®
Social and Behavioral Sciences Commons™
Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 2 of 2
Full-Text Articles in Social and Behavioral Sciences
Detection Of Al(Iii) And Ga(Iii) Complexes With Morin By Electrospray Ionization Mass Spectrometry, John B. Bremner, Larry A. Hick, Jody Morgan, Saowanee Rattanaphani, Vichitr Rattanaphani, C Septhum
Detection Of Al(Iii) And Ga(Iii) Complexes With Morin By Electrospray Ionization Mass Spectrometry, John B. Bremner, Larry A. Hick, Jody Morgan, Saowanee Rattanaphani, Vichitr Rattanaphani, C Septhum
Faculty of Science - Papers (Archive)
The Al(III) and Ga(III) complexes formed by morin (M) in aqueous solution were investigated by means of electrospray ionization mass spectrometry (ESI-MS). In the full scan mass spectra, Al:M showed 1:2 and 2:3 stoichiometric ratios. When (S)-N-acetylserine methyl ester (Ser), as a partial mimic of the serine residue in silk, was added to Al:M and Ga:M complexes in aqueous solution, the mass spectra of Ser:Al:M showed 1:1:1 and 1:1:2 stoichiometric ratios. The patterns of the mass spectra of Ga:M and Ser:Ga:M complexes were similar to those for the corresponding Al(III) complexes. Calculated heats of formation of potential structures of the …
Effect Of Protein Stabilization On Charge State Distribution In Positive- And Negative Ion Electrospray Ionization Mass Spectra, Stephen J. Watt, Margaret Sheil, Jennifer L. Beck, Pavel Prosselkov, Gottfried Otting, Nicholas E. Dixon
Effect Of Protein Stabilization On Charge State Distribution In Positive- And Negative Ion Electrospray Ionization Mass Spectra, Stephen J. Watt, Margaret Sheil, Jennifer L. Beck, Pavel Prosselkov, Gottfried Otting, Nicholas E. Dixon
Faculty of Science - Papers (Archive)
Changes in protein conformation are thought to alter charge state distributions observed in electrospray ionization mass spectra (ESI-MS) of proteins. In most cases, this has been demonstrated by unfolding proteins through acidification of the solution. This methodology changes the properties of the solvent so that changes in the ESI-MS charge envelopes from conformational changes are difficult to separate from the effects of changing solvent on the ionization process. A novel strategy is presented enabling comparison of ESI mass spectra of a folded and partially unfolded protein of the same amino acid sequence subjected to the same experimental protocols and conditions. …