ISSN:
0951-4198
Keywords:
Chemistry
;
Analytical Chemistry and Spectroscopy
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Physics
Notes:
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.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/rcm.1290080203
