title: Integration of residue-specific acid cleavage into proteomic workflows.
abstract: Microwave-accelerated proteolysis using acetic acid has been shown to occur specifically on either or both sides of aspartate residues. This chemical cleavage is applied to the yeast ribosome proteome to evaluate its suitability for incorporation into high-throughput automated workflows. Peptide product mixtures were analyzed using either an HPLC-ESI-LTQ-Orbitrap or an HPLC-MALDI-TOF2. The peptides were readily identified, using MASCOT with a modified enzyme rule, and provided information about 73% of the proteome. Implications are considered of the extended length and the presence of multiple basic residues in these peptides.
authors: Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA.
authors: Steven
authors: S
authors: Swatkoski
authors: Peter
authors: P
authors: Gutierrez
authors: Joy
authors: J
authors: Ginter
authors: Alexey
authors: A
authors: Petrov
authors: Jonathan D
authors: JD
authors: Dinman
authors: Nathan
authors: N
authors: Edwards
authors: Catherine
authors: C
authors: Fenselau
mesh_terms: D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D005656:Fungal Proteins / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods; D008872:Microwaves; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010455:Peptides / Q000737:chemistry*; D020543:Proteome; D040901:Proteomics / Q000379:methods*; D012270:Ribosomes / Q000737:chemistry / Q000378:metabolism; D021241:Spectrometry, Mass, Electrospray Ionization; D014357:Trypsin / Q000737:chemistry
chemical_list: D005656:Fungal Proteins; D010455:Peptides; D020543:Proteome; D014357:Trypsin