Charging of Proteins in Native Mass Spectrometry

Susa, Anna C.; Xia, Zijie; Tang, Henry Y.  H.; Tainer, John A.; Williams, Evan R.

doi:10.1007/s13361-016-1517-7

Title: Charging of Proteins in Native Mass Spectrometry

Journal Article · Wed Oct 12 00:00:00 EDT 2016 · Journal of the American Society for Mass Spectrometry

DOI:https://doi.org/10.1007/s13361-016-1517-7· OSTI ID:1421799

Susa, Anna C. ^[1]; Xia, Zijie ^[1]; Tang, Henry Y. H. ^[2]; Tainer, John A. ^[3]; Williams, Evan R. ^[1]

Univ. of California, Berkeley, CA (United States). Dept. of Chemistry
Univ. of California, Berkeley, CA (United States). Dept. of Chemistry; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biophysics and Integrated Bioimaging Division
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biophysics and Integrated Bioimaging Division; Univ. of Texas, Houston, TX (United States). M.D. Anderson Cancer Center, Dept. of Molecular and Cellular Oncology

Factors that influence the charging of protein ions formed by electrospray ionization from aqueous solutions in which proteins have native structures and function were investigated. Protein ions ranging in molecular weight from 12.3 to 79.7 kDa and pI values from 5.4 to 9.6 were formed from different solutions and reacted with volatile bases of gas-phase basicities higher than that of ammonia in the cell of a Fourier-transform ion cyclotron resonance mass spectrometer. The charge-state distribution of cytochrome c ions formed from aqueous ammonium or potassium acetate is the same. Moreover, ions formed from these two solutions do not undergo proton transfer to 2-fluoropyridine, which is 8 kcal/mol more basic than ammonia. These results provide compelling evidence that proton transfer between ammonia and protein ions does not limit protein ion charge in native electrospray ionization. Both circular dichroism and ion mobility measurements indicate that there are differences in conformations of proteins in pure water and aqueous ammonium acetate, and these differences can account for the difference in the extent of charging and proton-transfer reactivities of protein ions formed from these solutions. The extent of proton transfer of the protein ions with higher gas-phase basicity bases trends with how closely the protein ions are charged to the value predicted by the Rayleigh limit for spherical water droplets approximately the same size as the proteins. These results indicate that droplet charge limits protein ion charge in native mass spectrometry and are consistent with these ions being formed by the charged residue mechanism.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH)

Grant/Contract Number:: AC02-05CH11231; R01GM097357

OSTI ID:: 1421799

Journal Information:: Journal of the American Society for Mass Spectrometry, Vol. 28, Issue 2; ISSN 1044-0305

Publisher:: American Society for Mass SpectrometryCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 25 works

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37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Native mass spectrometry
ESI
Electrospray
Native ESI
Native mass spec
Native MS
Native electrospray
Electrospray ionization
Ammonium
Charging
Salts
Rayleigh limit
Charged residue mechanism
Gas-phase basicity
Apparent gas-phase basicity
Proton transfer
Combined charged residue-field emission model
Ion mobility
Circular dichroism
Mechanism
Charging mechanism
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Title: Charging of Proteins in Native Mass Spectrometry

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