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  2. Bottom-up proteomics - Wikipedia

    en.wikipedia.org/wiki/Bottom-up_proteomics

    Bottom-up proteomics is a common method to identify proteins and characterize their amino acid sequences and post-translational modifications by proteolytic digestion of proteins prior to analysis by mass spectrometry. [1] [2] BUP techniques can be an alternative to Maldi-Tof MS approaches, as they allow the identification of bacterial strains ...

  3. Shotgun proteomics - Wikipedia

    en.wikipedia.org/wiki/Shotgun_proteomics

    Tandem mass spectrometry is then used to identify the peptides. Targeted proteomics using SRM and data-independent acquisition methods are often considered alternatives to shotgun proteomics in the field of bottom-up proteomics. While shotgun proteomics uses data-dependent selection of precursor ions to generate fragment ion scans, the ...

  4. Proteomics - Wikipedia

    en.wikipedia.org/wiki/Proteomics

    Proteomics generally denotes the large-scale experimental analysis of proteins and proteomes, but often refers specifically to protein purification and mass spectrometry. Indeed, mass spectrometry is the most powerful method for analysis of proteomes, both in large samples composed of millions of cells [5] and in single cells. [6] [7]

  5. Top-down proteomics - Wikipedia

    en.wikipedia.org/wiki/Top-down_proteomics

    Top-down vs bottom-up proteomics. Top-down proteomics is a method of protein identification that either uses an ion trapping mass spectrometer to store an isolated protein ion for mass measurement and tandem mass spectrometry (MS/MS) analysis [1] [2] or other protein purification methods such as two-dimensional gel electrophoresis in conjunction with MS/MS. [3] Top-down proteomics is capable ...

  6. Isobaric labeling - Wikipedia

    en.wikipedia.org/wiki/Isobaric_labeling

    However, when fragmented during MS 2, in addition to the normal fragment ions, the reporter regions dissociate to produce ion signals that provide quantitative information regarding the relative amount of the peptide in the samples. Isobaric labeling is a mass spectrometry strategy used in quantitative proteomics.

  7. Electron-capture dissociation - Wikipedia

    en.wikipedia.org/wiki/Electron-capture_dissociation

    Electron-capture dissociation (ECD) is a method of fragmenting gas-phase ions for structure elucidation of peptides and proteins in tandem mass spectrometry. It is one of the most widely used techniques for activation and dissociation of mass selected precursor ion in MS/MS.

  8. Mass spectrum - Wikipedia

    en.wikipedia.org/wiki/Mass_spectrum

    A mass spectrum is a histogram plot of intensity vs. mass-to-charge ratio (m/z) in a chemical sample, [1] usually acquired using an instrument called a mass spectrometer. Not all mass spectra of a given substance are the same; for example, some mass spectrometers break the analyte molecules into fragments ; others observe the intact molecular ...

  9. Mass spectrometric immunoassay - Wikipedia

    en.wikipedia.org/wiki/Mass_spectrometric_immunoassay

    Mass spectrometric immunoassay (MSIA) is a rapid method is used to detect and/ or quantify antigens and or antibody analytes. [1] This method uses an analyte affinity (either through antigens or antibodies) isolation to extract targeted molecules and internal standards from biological fluid in preparation for matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI ...