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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2003-9-29
pubmed:abstractText
Collision-induced fragmentations of deprotonated maculatin 1 peptides provide significant sequencing information. When the peptide lacks those residues which can fragment through their alpha side chains (e.g. Thr, Ser, Glu and Gln in this study) the basic alpha and beta' backbone cleavages occur from the [Mbond;H](-) anion. When Thr, Ser, Glu and Gln are present, the ease of side-chain fragmentation of these residues is: Thr (loss of MeCHO) > Ser (CH(2)O) > Glu (H(2)O) > Gln (NH(3)). When one of more of these residues is (are) present, the alpha and beta' cleavages often occur from a fragment rather than the [Mbond;H](-) anion, e.g. for Thr, the [(Mbond;H)(-)bond;MeCHO](-) anion. These four residues also initiate gamma backbone cleavage reactions. The relative abundances of peaks resulting from gamma cleavage are Glu > Ser = Thr > Gln for maculatin 1 spectra. An unusual Gln19/Ile17 cyclisation/cleavage reaction occurs in maculatin spectra: the peptide [Mbond;H](-) anion must adopt a helical conformation in order for these two groups to interact. Analogous fragmentations have been reported previously in the negative ion spectra of the caerin 1 peptides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0951-4198
pubmed:author
pubmed:copyrightInfo
Copyright 2003 John Wiley & Sons, Ltd.
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2215-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Negative ion electrospray mass spectra of the maculatin peptides from the tree frogs Litoria genimaculata and Litoria eucnemis.
pubmed:affiliation
Department of Chemistry, The University of Adelaide, South Australia, 5005. john.bowie@adelaide.edu.au
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't