Dissociation behavior of doubly-charged tryptic peptides: correlation of gas-phase cleavage abundance with ramachandran plots.
Analysis of fragmentation patterns from 5654 unique doubly charged tryptic peptides is obtained. Great variability of average relative abundance of bond cleavage is found between different amino acid combinations. There exist similarities as well as differences between b and y ions. Strong enhancement or suppression of cleavage gives insight into possible chemical interactions at reactive conformations formed by preferred phi-psi angles.
Huang
Yingying
Y
Department of Chemistry, University of Arizona, Tucson, Arizona 85721, USA.
Triscari
Joseph M
JM
Pasa-Tolic
Ljiljana
L
Anderson
Gordon A
GA
Lipton
Mary S
MS
Smith
Richard D
RD
Wysocki
Vicki H
VH
D000596:Amino Acids / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry*; D003626:Data Display; D005740:Gases; D013058:Mass Spectrometry; D010446:Peptide Fragments / Q000737:chemistry*; D020543:Proteome / Q000737:chemistry; D020592:Shewanella / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry* / Q000378:metabolism
D000596:Amino Acids; D001426:Bacterial Proteins; D005740:Gases; D010446:Peptide Fragments; D020543:Proteome; D014357:Trypsin