Temple University MASS SPECTROMETRY FURTHER INVESTIGATIONS Ilyana Mushaeva and Amber Moscato Department of Electrical and Computer Engineering Temple University.

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Presentation transcript:

Temple University MASS SPECTROMETRY FURTHER INVESTIGATIONS Ilyana Mushaeva and Amber Moscato Department of Electrical and Computer Engineering Temple University

Temple University: Slide 1 How is the Mass Spectrum Analyzed? C = 12 m/z CH = 13 m/z = 14 m/z = 15 m/z = 26 m/z = 27 m/z = 28 m/z = 39 m/z = 40 m/z = 41 m/z = 42 m/z = 43 m/z has m/z of 42, so why does a peak at 43 exist? The M+1 peak exists because Carbon has 3 Isotopes (same element with different neutrons and amu). Carbon-13 is rare, but shows up in this spectrum. Generally, these peaks are neglected because Carbon 12 is more common (98%).

Temple University: Slide 2 Signal Processing in Relation to MS/MS Database of Protein Sequences can be used as a pattern recognition technique to determine the proteins we are working with. Software exists that evaluates protein sequences from a database to determine which peptides (amino acid links) could be present. Can a model be constructed using cross correlation or filtering techniques? Problem: The possible number of proteins in existence form an exponential of and for every protein, there is another that can break it down!

Temple University: Slide 3 Database for Detection? Searching a database allows for a decrease in falsely determined peaks. Generate an ROC curve, which provides a visual for correctly detected peaks vs. falsely detected peaks (cross correlation technique). ID proteins from peptide (amino acids)

Temple University: Slide 4 The Data Why is this precursor selected? Is it Metastable and needs further analysis? PeakIntensity = PeakMass =

Temple University: Slide 5 Fragments resulting from MS of Precursor The Data

Temple University: Slide 6 The Ionization Process The Ionization Process – when an electron is accelerated through an electric field, it gains kinetic energy. Electrons accelerate through an Electric Field of 70 V and gain kinetic energy of 70 eV. They interact with neutral molecules to remove an electron from it. These two electrons exit, leaving behind the Molecular Ion (highest mass-to-charge ratio). Fragment Ions are formed when there is an excess of energy within the Molecular Ion. This explains why the fragments contain smaller masses.

Temple University: Slide 7 Tandem Mass Spectrometry There is an initial kinetic energy within the Precursor Ion. Enters the Collision Induced Dissociation Region (Precursor Ion collides with a Neutral gas) and fragments (products) result. The fragment ions are deflected at angles as a result of an electric field, which is varied depending on individual Ion masses. Metastable Ions are those that contain the kinetic energies, and enter a Time of Flight analyzer.

Temple University: Slide 8 Brief Bibliography I. Kaltashov and S. Eyles. Mass Spectrometry in Biophysics. Wiley- Interscience M. Baldwin. Protein Identification by Mass Spectrometry available at C. G. Herbert and R. A. W. Johnstone. Mass Spectrometry Basics. CRC Press LLC Understanding Chemistry. Available at S.A. Trauger and W. Webb. Peptide and protein analysis with mass spectrometry. The Scripps Research Institute Available at