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  2. Bottom-up proteomics - Wikipedia

    en.wikipedia.org/wiki/Bottom-up_proteomics

    Essentially, bottom-up proteomics is a relatively simple and reliable means of determining the protein make-up of a given sample of cells, tissues, etc. [5] In bottom-up proteomics, the crude protein extract is enzymatically digested, followed by one or more dimensions of separation of the peptides by liquid chromatography coupled to mass ...

  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. 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 ...

  5. Mass spectrometry - Wikipedia

    en.wikipedia.org/wiki/Mass_spectrometry

    Ion mobility spectrometry-mass spectrometry (IMS/MS or IMMS) is a technique where ions are first separated by drift time through some neutral gas under an applied electrical potential gradient before being introduced into a mass spectrometer. [43] Drift time is a measure of the collisional cross section relative to the charge of the ion.

  6. Protein mass spectrometry - Wikipedia

    en.wikipedia.org/wiki/Protein_mass_spectrometry

    A mass spectrometer used for high throughput protein analysis. Protein mass spectrometry refers to the application of mass spectrometry to the study of proteins.Mass spectrometry is an important method for the accurate mass determination and characterization of proteins, and a variety of methods and instrumentations have been developed for its many uses.

  7. Electron-capture dissociation - Wikipedia

    en.wikipedia.org/wiki/Electron-capture_dissociation

    Schematic diagram of the combined ECD FTICRMS and IRMPD experimental setup. 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 ...

  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. Droplet-based microfluidics - Wikipedia

    en.wikipedia.org/wiki/Droplet-based_Microfluidics

    Mass spectrometry (MS) is a near universal detection technique that is recognized throughout the world as the gold standard for identification of manycompounds. MS is an analytical technique in which chemical species are ionized and sorted before detection, and the resulting mass spectrum is used to identify the ions' parent molecules.