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  3. List of mass spectrometry software - Wikipedia

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

    Swiss Mass Abacus is a calculator of peptide and glycopeptide masses. It is purposefully kept as simple as a basic calculator executing arithmetic operations. TOF-DS Proprietary: Software by Markes International used with BenchTOF time-of-flight mass spectrometers. TopFD Open source

  4. Mascot (software) - Wikipedia

    en.wikipedia.org/wiki/Mascot_(software)

    Mascot identifies proteins by interpreting mass spectrometry data. The prevailing experimental method for protein identification is a bottom-up approach, where a protein sample is typically digested with trypsin to form smaller peptides.

  5. Delta-sleep-inducing peptide - Wikipedia

    en.wikipedia.org/wiki/Delta-sleep-inducing_peptide

    Delta-sleep-inducing peptide (DSIP) is a neuropeptide that when infused into the mesodiencephalic ventricle of recipient rabbits induces spindle and delta EEG activity and reduced motor activities. [1] Its amino acid sequence is Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu (WAGGDASGE). The gene has yet to be found in rabbits, along with any receptors or ...

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  7. Label-free quantification - Wikipedia

    en.wikipedia.org/wiki/Label-free_quantification

    Label-free quantification is a method in mass spectrometry that aims to determine the relative amount of proteins in two or more biological samples. Unlike other methods for protein quantification , label-free quantification does not use a stable isotope containing compound to chemically bind to and thus label the protein.

  8. PeptideAtlas - Wikipedia

    en.wikipedia.org/wiki/PeptideAtlas

    PeptideAtlas is a proteomics data resource that gathers tandem mass spectrometry datasets from around the world, reprocesses them with the Trans-Proteomic Pipeline, and makes the combined result freely available to the community.

  9. 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).