Linked Life Data

8875591

Source:http://linkedlifedata.com/resource/pubmed/id/8875591

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-2-3
pubmed:abstractText
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), a method well-suited for mass determination of biomolecules, has been used to analyze fragment ions generated by post-source decay (PSD) of synthetic peptaibols containing high proportions of the sterically hindered amino acids alpha-amino isobutyric acid (Aib) and isovaline (Iva). Since peptaibols do not have a free N-terminal amino group or side chains subject to protonation, the analyzed peptides saturnisporin SA III, trichotoxin A-50 and chrysospermin B were shown to provide preferred N-terminal and C-terminal a, b, and y fragments as sodium adduct. Additionally, a cleavage of the labile Aib-Probond was observed for all peptides investigated. The fragmentation pattern allowed confirmation of the primary structure and, therefore, demonstrated the usefulness of MALDI-PSD mass spectrometry for sequence analysis of the peptaibols.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1040-5704
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
122-6
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:articleTitle
Mass spectrometric sequencing of synthetic peptides containing alpha, alpha-dialkylated amino acid residues by MALDI post-source decay analysis.
pubmed:affiliation
Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.
pubmed:publicationType
Journal Article