期刊
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
卷 22, 期 11, 页码 1968-1977出版社
SPRINGER
DOI: 10.1007/s13361-011-0218-5
关键词
Anion; Sodium; Adduction; Electrospray; Hofmeister series; Proteins
资金
- National Science Foundation [CHE-1012833]
- National Institutes of Health [5F32GM093593-02]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1012833] Funding Source: National Science Foundation
Gaseous protein-metal ion and protein-molecule complexes can be readily formed by electrospray ionization (ESI) from aqueous solutions containing proteins and millimolar concentrations of sodium salts of various anions. The extent of sodium and acid molecule adduction to multiply charged protein ions is inversely related and depends strongly on the proton affinity (PA) of the anion, with extensive sodium adduction occurring for anions with PA values greater than similar to 300 kcal.mol(-1) and extensive acid molecule adduction occurring for anions with PA values less than 315 kcal.mol(-1). The role of the anion on the extent of sodium and acid molecule adduction does not directly follow the Hofmeister series, suggesting that direct protein-ion interactions may not play a significant role in the observed effect of anions on protein structure in solution. These results indicate that salts with anions that have low PA values may be useful solution-phase additives to minimize nonspecific metal ion adduction in ESI experiments designed to identify specific protein-metal ion interactions.
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