title: Mass spectrometric signature of S-prenylated cysteine peptides.
abstract: The fast atom bombardment mass spectra of peptides containing S-prenylated cysteine display signature fragmentations characteristic of this modified amino acid. The fragmentation is independent of the nature of the cysteine carbonyl substituent, easily differentiates prenyl from nonprenyl alkylation, and readily identifies the oligomer count of the prenyl. This screening method, which requires little time, effort, or material (compared with previous analysis methods based on chemical degradation), greatly facilitates the identification of these prenylated proteins.
authors.affiliation: Department of Chemistry, University of Tennessee, Knoxville 37996.
authors.forename: A A
authors.initials: AA
authors.lastname: Tuinman
authors.forename: D A
authors.initials: DA
authors.lastname: Thomas
authors.forename: K D
authors.initials: KD
authors.lastname: Cook
authors.forename: C B
authors.initials: CB
authors.lastname: Xue
authors.forename: F
authors.initials: F
authors.lastname: Naider
authors.forename: J M
authors.initials: JM
authors.lastname: Becker
mesh_terms: D000595:Amino Acid Sequence; D003545:Cysteine / Q000737:chemistry*; D000072235:Mating Factor; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011499:Protein Processing, Post-Translational; D016339:Spectrometry, Mass, Fast Atom Bombardment
chemical_list: D009842:Oligopeptides; D010446:Peptide Fragments; D010455:Peptides; D000072235:Mating Factor; D003545:Cysteine