[madscientist]

Hi all,

Im trying to design an experiment involving peptide sequencing via the Edman degradation reaction. 

If i had a simple peptide such as Asp - Leu - Lys which amino acid would be cleaved/removed first?

I know it involves attachment of the peptide terminal amino group to phenyl isothiocyanate (PITC) which yeilds an N-phenylthiourea derivative,  but am unsure as to which end of the peptide this occurs at. i.e does PITC join to the N in Asp or the N in Lys (see above sequence)

The entire reaction is shown below, any help or hints would be much appreciated

Cheers,

[Dan]

It's been a while, but I seem to remember that peptides are always named (left to right) from the N terminus to the C terminus.

[madscientist]

Sweet, thanks Dan