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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. 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.

  5. 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]

  6. 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.

  7. De novo peptide sequencing - Wikipedia

    en.wikipedia.org/wiki/De_novo_peptide_sequencing

    In mass spectrometry, de novo peptide sequencing is the method in which a peptide amino acid sequence is determined from tandem mass spectrometry. Knowing the amino acid sequence of peptides from a protein digest is essential for studying the biological function of the protein. In the old days, this was accomplished by the Edman degradation ...

  8. 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 ...

  9. Talk:Bottom-up proteomics - Wikipedia

    en.wikipedia.org/wiki/Talk:Bottom-up_proteomics

    But peptide mass fingerprinting is a distinct technique that doesn't involve tandem mass spectrometry. – CWenger ( ^ • @ ) 16:01, 1 May 2023 (UTC) [ reply ] The peptide mass fingerprinting page mentions MS/MS in several places (including the main figure), so the distinction may not be that clear.