Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10537015 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2013 | 11 Pages |
Abstract
4-Hydroxy-2-(E)-nonenal addition to porcine mitochondrial aconitase was investigated using mass spectrometry. Identified Michael addition sites are in red; underscores indicate sites detected with both ion trap and Orbitrap instruments (highest confidence). 94.2% sequence coverage was achieved using trypsin and chymotrypsin (trypsin only highlighted blue, chymotrypsin only highlighted yellow, and both enzymes highlighted green).469
Keywords
HNETris-buffered saline containing 0.05% Tween 20peptide-spectrum matchTrans-proteomic pipelineACO2PSMTBSTHCDMWCODTTFDRTPPCIDMitochondrial aconitaseCollision-induced dissociationtrans-4-Hydroxy-2-nonenalSASAdithiothreitolsolvent-accessible surface areaMass spectrometryfalse discovery ratemolecular weight cut-offProtein carbonylation
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Qingyuan Liu, David C. Simpson, Scott Gronert,