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  2. List of mass spectrometry software - Wikipedia

    en.wikipedia.org/wiki/List_of_mass_spectrometry...

    This automated quantitative Data-independent acquisition-proteomics software, developed by the Demichev and Ralser labs at the Charité in Berlin, Germany, implements a machine-learning algorithm based on an ensemble of deep neural networks, to boost proteomic depth and reliability of peptide and protein identification. DIA-NN is optimized for ...

  3. De novo peptide sequencing - Wikipedia

    en.wikipedia.org/wiki/De_novo_peptide_sequencing

    The possible peptide that has the most similar spectrum will have the highest chance to be the right sequence. However, the number of possible peptides may be large. For example, a precursor peptide with a molecular weight of 774 has 21,909,046 possible peptides. Even though it is done in the computer, it takes a long time. [17] [18]

  4. Protein sequencing - Wikipedia

    en.wikipedia.org/wiki/Protein_sequencing

    Protein sequence interpretation: a scheme new protein to be engineered in a yeast. It is often desirable to know the unordered amino acid composition of a protein prior to attempting to find the ordered sequence, as this knowledge can be used to facilitate the discovery of errors in the sequencing process or to distinguish between ambiguous results.

  5. Peptide microarray - Wikipedia

    en.wikipedia.org/wiki/Peptide_microarray

    A peptide microarray is a planar slide with peptides spotted onto it or assembled directly on the surface by in-situ synthesis. Whereas peptides spotted can undergo quality controls that include mass spectrometer analysis and concentration normalization before spotting and result from a single synthetic batch, peptides synthesized directly on the surface may suffer from batch-to-batch ...

  6. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).

  7. Peptide mass fingerprinting - Wikipedia

    en.wikipedia.org/wiki/Peptide_mass_fingerprinting

    A typical workflow of a peptide mass fingerprinting experiment. Peptide mass fingerprinting (PMF), also known as protein fingerprinting, is an analytical technique for protein identification in which the unknown protein of interest is first cleaved into smaller peptides, whose absolute masses can be accurately measured with a mass spectrometer such as MALDI-TOF or ESI-TOF. [1]

  8. Liquid chromatography–mass spectrometry - Wikipedia

    en.wikipedia.org/wiki/Liquid_chromatography...

    This tandem technique can be used to analyze biochemical, organic, and inorganic compounds commonly found in complex samples of environmental and biological origin. Therefore, LC–MS may be applied in a wide range of sectors including biotechnology, environment monitoring, food processing, and pharmaceutical, agrochemical, and cosmetic industries.

  9. Peptide computing - Wikipedia

    en.wikipedia.org/wiki/Peptide_computing

    Peptide computing is a form of computing which uses peptides, instead of traditional electronic components. The basis of this computational model is the affinity of antibodies towards peptide sequences. Similar to DNA computing, the parallel interactions of peptide sequences and antibodies have been used by this model to solve a few NP-complete ...