Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-4-23
pubmed:abstractText
The abundance distribution of multiply charged ions produced during the electrospray process is thought to depend on the initial conformational state of the analyte in solution and on solution chemistry, but with some proteins, including apomyoglobin, the correlation between solution and mass spectrometry data is unclear. In this study, we compare our results obtained by mass spectrometry with available data describing conformations and average number of charges of apomyoglobin in solution. A good correlation between average number of charges in solution and in the mass spectrum is only found for the pH 4.2 solution. We propose that the discrepancies between solution and electrospray ionization mass spectrometry observed with apomyoglobin under other solution conditions can be mainly explained by (1) a preferential fragmentation of the highly charged ions in the source and (2) a variation of pH in the droplets during the electrospray process.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0951-4198
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
239-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
On the origin of the abundance distribution of apomyoglobin multiply charged ions in electrospray mass spectrometry.
pubmed:affiliation
Mass Spectrometry Laboratory, Chemistry Institute B6, Liège University, Belgium.
pubmed:publicationType
Journal Article