Electrothermal supercharging in mass spectrometry and tandem mass spectrometry of native proteins.

ABSTRACT: Electrothermal supercharging of protein ions formed by electrospray ionization from buffered aqueous solutions results in significant increases to both the maximum and average charge states compared to native mass spectrometry in which ions are formed from the same solutions but with lower spray potentials. For eight of the nine proteins investigated, the maximum charge states of protonated ions formed from native solutions with electrothermal supercharging is greater than those obtained from conventional denaturing solutions consisting of water/methanol/acid, although the average charging is slightly lower owing to contributions of small populations of more folded low charge-state structures. Under these conditions, electrothermal supercharging is slightly less effective for anions than f

SUBMITTER: Cassou CA 

PROVIDER: S-EPMC3536820 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature