title: Peptide mass fingerprinting: identification of proteins by MALDI-TOF.
abstract: MALDI-TOF peptide mass fingerprinting (PMF) is the fastest and cheapest method of protein identification; the studied genome is sequenced and annotated, and the protein is amenable to separation and detection in 2D gel electrophoresis. In plant proteomics there are two main difficulties: few plant genomes are sequenced, and major contaminants are non-plant specific. This chapter describes the classical "bottom-up" method (i.e., from peptide to protein identification) of gel cutting, in-gel digestion, peptide recovery and purification, MALDI-TOF mass spectrometry, and critical survey of protein database queries.
authors.affiliation: Laboratoire de Protéomique, INRA, Montpellier, France.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Sommerer
authors.forename: Delphine
authors.initials: D
authors.lastname: Centeno
authors.forename: Michel
authors.initials: M
authors.lastname: Rossignol
mesh_terms: D000180:Acrylic Resins; D019295:Computational Biology / Q000379:methods; D030562:Databases, Protein; D015180:Electrophoresis, Gel, Two-Dimensional; D010449:Peptide Mapping / Q000379:methods*; D010940:Plant Proteins / Q000032:analysis* / Q000737:chemistry / Q000302:isolation & purification; D010944:Plants / Q000737:chemistry; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
chemical_list: D000180:Acrylic Resins; D010940:Plant Proteins; C016680:polyacrylamide gels