ArticleJournal of the American Society for Mass Spectrometry2005
Direct correlation of the crystal structure of proteins with the maximum positive and negative charge states of gaseous protein ions produced by electrospray ionization.
Article in Journal of the American Society for Mass Spectrometry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Predicting the Solubility of Amino Acids and Peptides with the SAFT-γ Mie Approach: Neutral and Charged Models.Industrial & engineering chemistry research · 2024Article
- Salt Bridge Rearrangement (SaBRe) Explains the Dissociation Behavior of Noncovalent Complexes.Journal of the American Society for Mass Spectrometry · 2016Article
- Susceptibility of Mutant SOD1 to Form a Destabilized Monomer Predicts Cellular Aggregation and Toxicity but NotFrontiers in neuroscience · 2016Article
- What protein charging (and supercharging) reveal about the mechanism of electrospray ionization.Journal of the American Society for Mass Spectrometry · 2014Article
- Selective deletion of the internal lysine residue from the peptide sequence by collisional activation.Journal of the American Society for Mass Spectrometry · 2012Article
- A computational model for protein ionization by electrospray based on gas-phase basicity.Journal of the American Society for Mass Spectrometry · 2012Article
- Electrospray ionization mass spectrometry: a technique to access the information beyond the molecular weight of the analyte.International journal of analytical chemistry · 2012Article
- Evidence of molecular fragmentation inside the charged droplets produced by electrospray process.Journal of the American Society for Mass Spectrometry · 2011Article
- Total chemical synthesis of biologically active vascular endothelial growth factor.Angewandte Chemie (International ed. in English) · 2011Article
- On the zwitterionic nature of gas-phase peptides and protein ions.PLoS computational biology · 2010Article
- Modifying the charge state distribution of proteins in electrospray ionization mass spectrometry by chemical derivatization.Journal of the American Society for Mass Spectrometry · 2009Article
- Investigation of deprotonation reactions on globular and denatured proteins at atmospheric pressure by ESSI-MS.Journal of the American Society for Mass Spectrometry · 2008Article
- Metal-binding properties of human centrin-2 determined by micro-electrospray ionization mass spectrometry and UV spectroscopy.Journal of the American Society for Mass Spectrometry · 2006Article
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
Electrospray mass spectrometric studies in native folded forms of several proteins in aqueous solution have been performed in the positive and negative ion modes. The mass spectra of the proteins show peaks corresponding to multiple charge states of the gaseous protein ions. The results have been analyzed using the known crystal structures of these proteins. Crystal structure analysis shows that among the surface exposed residues some are involved in hydrogen-bonding or salt-bridge interactions while some are free. The maximum positive charge state of the gaseous protein ions was directly related to the number of free surface exposed basic groups whereas the maximum negative charge state was related to the number of free surface exposed acidic groups of the proteins. The surface exposed basic groups, which are involved in hydrogen bonding, have lower propensity to contribute to the positive charge of the protein. Similarly, the surface exposed acidic groups involved in salt bridges have lower propensity to contribute to the negative charge of the protein. Analysis of the crystal structure to determine the maximum charge state of protein in the electrospray mass spectrum was also used to interpret the reported mass spectra of several proteins. The results show that both the positive and the negative ion mass spectra of the proteins could be interpreted by simple consideration of the crystal structure of the folded proteins. Moreover, unfolding of the protein was shown to increase the positive charge-state because of the availability of larger number of free basic groups at the surface of the unfolded protein.
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