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Selected Protocol from "Proteins and Proteomics: A Laboratory Manual", Richard J. Simpson.
General Method for MALDI-MS Analysis of Proteins and Peptides
David Frecklington
Joint Proteomics Laboratory (JPSL)
Ludwig Institute for Cancer Research
Walter and Eliza Hall Institute of Medical Research
Melbourne, Australia
ABSTRACT
For MALDI-TOF-MS analysis of proteins and peptides, samples are cocrystallized with an excess of organic matrix that absorbs at a specific wavelength (usually, UV337nm). Typically, sinapinic acid (SA) is the matrix of choice for large proteins, whereas {alpha}-cyano-4-hydroxy-cinnamic acid (HCCA) is the preferred matrix for peptide mapping. Following a short laser pulse, analytes are protonated and desorbed into the gas phase, and their m/z values are determined in a TOF mass analyzer. Mass accuracy determinations vary from ±0.01% to 0.1% depending on the sample preparation technique and the method used for mass calibration. |
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