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Topic: ideal molecular weight of peptides in LC  (Read 1855 times)

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Offline Babcock_Hall

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ideal molecular weight of peptides in LC
« on: August 02, 2012, 12:46:30 PM »
We are planning to use a protease to identify the site of chemical modification in a protein that should result in the modification of a cysteine by about 94 mass units.  We are thinking both in  terms of RP HPLC for peptide mapping and also in terms of possibly doing LC/MS of some sort.  We often detect proteins in similar experiments by their absorbance at 215 nm.  Trypsin is predicted to give a hexapeptide and LysC is predicted to give a 22-mer.  Is a hexapeptide too small to observe by UV detection?  Does anyone have any thoughts on the 22-mer?  Thanks.

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