You have isolated the proteins from two adjacent spots after two-dimensional
Chapter 0, Problem 8-11(choose chapter or problem)
You have isolated the proteins from two adjacent spots after two-dimensional polyacrylamide-gel electrophoresis and digested them with trypsin. When the masses of the peptides were measured by MALDI-TOF mass spectrometry, the peptides from the two proteins were found to be identical except for one (Figure Q82). For this peptide, the mass-to-charge (m/z) values differed by 80, a value that does not correspond to a difference in amino acid sequence. (For example, glutamic acid instead of valine at one position would give an m/z difference of around 30.) Can you suggest a possible difference between the two peptides that might account for the observed m/z difference?
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