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Probing conformational changes in some proteins by positive‐ion electrospray mass spectrometry
Author(s) -
Hamdan M.,
Curcuruto O.
Publication year - 1994
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290080203
Subject(s) - chemistry , electrospray , aqueous solution , ion , mass spectrometry , analytical chemistry (journal) , mass spectrum , charge (physics) , electrospray ionization , chromatography , organic chemistry , physics , quantum mechanics
Charge‐state distributions in the positive‐ion electrospray (ES + ) mass spectra of some proteins are monitored at various temperatures of the ion source. The observed shifts in charge‐state profiles favouring higher charge‐states are linked to heat‐induced conformations cited by other research groups. To gain more insight into the origin of the observed shifts, a number of measurements were also performed at different flow rates of the electrospray drying gas, on both aqueous and organic solutions of protein. The flow rate of the drying gas was found to influence the relative intensities of high charge‐states induced by heat or organic solvents to a small extent, but it did not produce substantial shifts in the charge‐state distributions observed in room temperatures ES + mass spectra of aqueous solutions.