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Edman chemistry coupling

Many structural biology and biochemistry studies rely on the precise identification of the N-/C-terminal sequence of a protein (e.g., signal peptide identification, determining the cleavage site and specificity of a novel protease, etc.). Digestion of proteins in arrays of carboxypeptidase Y at different concentrations with MALDl-MS-based readout can be employed to derive C-terminal sequence information for proteins. The amino-terminus of a protein can be derived by wet chemistries similar to Edman degradation coupled to MS-readout. This method of protein ladder sequencing, reported first by Kent and... [Pg.695]


See other pages where Edman chemistry coupling is mentioned: [Pg.75]    [Pg.91]    [Pg.366]    [Pg.3]    [Pg.114]    [Pg.3919]    [Pg.3920]    [Pg.181]    [Pg.271]    [Pg.177]    [Pg.38]    [Pg.3042]    [Pg.61]    [Pg.279]   
See also in sourсe #XX -- [ Pg.3 ]




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