ArticleJournal of the American Society for Mass Spectrometry2001
The methanol-induced conformational transitions of beta-lactoglobulin, cytochrome c, and ubiquitin at low pH: a study by electrospray ionization mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 72 citations in OpenAlex.
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- Biophysical characterization of the inactivation of E. coli transketolase by aqueous co-solvents.Scientific reports · 2021Article
- Characterization of Intramolecular Interactions of Cytochrome c Using Hydrogen-Deuterium Exchange-Trapped Ion Mobility Spectrometry-Mass Spectrometry and Molecular Dynamics.Analytical chemistry · 2017Article
- Lid opening and conformational stability of T1 Lipase is mediated by increasing chain length polar solvents.PeerJ · 2017Article
- Nano-Armoring of Enzymes: Rational Design of Polymer-Wrapped Enzymes.Methods in enzymology · 2017Article
- To What Extent is FAIMS Beneficial in the Analysis of Proteins?Journal of the American Society for Mass Spectrometry · 2016Article
- Changes in protein structure monitored by use of gas-phase hydrogen/deuterium exchange.Proteomics · 2015Article
- How ubiquitin unfolds after transfer into the gas phase.Journal of the American Society for Mass Spectrometry · 2012Article
- Electrothermal supercharging of proteins in native electrospray ionization.Analytical chemistry · 2012Article
- Investigating the role of adducts in protein supercharging with sulfolane.Journal of the American Society for Mass Spectrometry · 2012Article
- Mass-spectrometric characterization of cisplatin binding sites on native and denatured ubiquitin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- Electrospray droplet exposure to gaseous acids for the manipulation of protein charge state distributions.Analytical chemistry · 2010Article
- Irreversible thermal denaturation of cytochrome C studied by electrospray mass spectrometry.Journal of the American Society for Mass Spectrometry · 2009Article
- Conformations of gas-phase ions of ubiquitin, cytochrome c, apomyoglobin, and beta-lactoglobulin produced from two different solution conformations.Journal of the American Society for Mass Spectrometry · 2008Article
- Gas phase noncovalent protein complexes that retain solution binding properties: Binding of xylobiose inhibitors to the beta-1, 4 exoglucanase from cellulomonas fimi.Journal of the American Society for Mass Spectrometry · 2007Article
- Monoclonal antibodies against Enterocytozoon bieneusi of human origin.Clinical and diagnostic laboratory immunology · 2005Article
- Direct correlation of the crystal structure of proteins with the maximum positive and negative charge states of gaseous protein ions produced by electrospray ionization.Journal of the American Society for Mass Spectrometry · 2005Article
- Generation of mass tags by the inherent electrochemistry of electrospray for protein mass spectrometry.Journal of the American Society for Mass Spectrometry · 2004Review
- E. coli trp repressor forms a domain-swapped array in aqueous alcohol.Structure (London, England : 1993) · 2004Article
- Detecting equilibrium cytochrome c folding intermediates by electrospray ionisation mass spectrometry: two partially folded forms populate the molten-globule state.Protein science : a publication of the Protein Society · 2002Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The methanol-induced conformational transitions under acidic conditions for beta-lactoglobulin, cytochrome c, and ubiquitin, representing three different classes of proteins with beta-sheets, alpha-helices, and both alpha-helices and beta-sheets, respectively, are studied under equilibrium conditions by electrospray ionization mass spectrometry (ESI-MS). The folding states of proteins in solution are monitored by the charge state distributions that they produce during ESI and by hydrogen/deuterium (H/D) exchange followed by ESI-MS. The changes in charge state distributions are correlated with earlier studies by optical and other methods which have shown that, in methanol, these proteins form partially unfolded intermediates with induced alpha-helix structure. Intermediate states formed at about 35% methanol concentration are found to give bimodal charge state distributions. The same rate of H/D exchange is shown by the two contributions to the bimodal distributions. This suggests the intermediates are highly flexible and may consist of a mixture of two or more rapidly interconverting conformers. H/D exchange of proteins followed by ESI-MS shows that helical denatured states, populated at around 50% methanol concentration, transform into more protected structures with further increases in methanol concentration, consistent with previous circular dicroism studies. These more protected structures still produce high charge states in ESI, similar to those of the fully denatured proteins.
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