title: Determination of post-translational modifications of proteins by high-sensitivity, high-resolution Fourier transform ion cyclotron resonance mass spectrometry.
abstract: The response of a cell to its extracellular environment is a multi-step process beginning with signal transduction that is governed by "subtle changes" often resulting in protein expression. Proteomics is the tracking of this protein expression. Post-translational modification (PTM) is a "subtle change" that has a major influence on signal transduction. Phosphorylation and glycosylation propagate signals by sequential, reversible modifications. High-sensitivity, high-resolution and multiple MS capabilities of Fourier transform ion cyclotron resonance mass spectrometry permit localization of the PTM(s) with electron-capture dissociation, and then structural determination of the PTM with infrared multiphoton dissociation.
authors: National High Magnetic Field Laboratory, Florida State University, B224 Magnet Laboratory, 1800 E. Paul Dirac Drive, Tallahassee, FL 32310-3706, USA. emmett@magnet.fsu.edu
authors: Mark R
authors: MR
authors: Emmett
mesh_terms: D000595:Amino Acid Sequence; D002240:Carbohydrate Sequence; D002241:Carbohydrates / Q000737:chemistry; D015180:Electrophoresis, Gel, Two-Dimensional; D006023:Glycoproteins / Q000737:chemistry; D006031:Glycosylation; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D012680:Sensitivity and Specificity; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D002241:Carbohydrates; D006023:Glycoproteins