Applying ion-molecule reactions to studies of gas-phase protein structure
Whether solution phase differences in protein higher order structure persist in the gas phase, is examined by means of proton transfer reactions on ions generated by electrospray ionization of different solution conformations. Ion-molecule reactions were carried out in the atmosphere-vacuum interface of a quadrupole mass spectrometer with a Y-shaped capillary inlet-reactor. An amine (dimethyl-, trimethyl-, or diethyl-) were delivered to one inlet arm. Reactivities of bovine cytochrome c ions sprayed from denatured and native solutions were determined; the ions generated shifted to about the same charge states. Addition of equal amounts of amine to ions generated from different solution conformations of bovine ubiquitin also yielded similar final charge states; however, the average charge state increased with temperature. Myoglobin and apomyoglobin also yielded similar final charge states. The results suggest that for the non-disulfide linked proteins, either there are not significant differences in gas phase higher order structure, or proton transfer reactions are not sensitive enough to detect higher order structural differences arising from noncovalent interactions. 2 refs, 2 figs. (DLC)
- Research Organization:
- Pacific Northwest Lab., Richland, WA (United States)
- Sponsoring Organization:
- USDOE, Washington, DC (United States)
- DOE Contract Number:
- AC06-76RL01830
- OSTI ID:
- 10170983
- Report Number(s):
- PNL-SA-20437; CONF-9205196-7; ON: DE92019131
- Resource Relation:
- Conference: 40. American Society for Mass Spectrometry (ASMS) conference on mass spectrometry and allied topics,Washington, DC (United States),31 May - 2 Jun 1992; Other Information: PBD: Jun 1992
- Country of Publication:
- United States
- Language:
- English
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