[diablo]

Hi folks,

i'm still working @ the same experiment and i got a question :

I've taken a small protein (Albumin) and performed trypsin digestion. After that i've added some BOC and Base (DIPEA) and incubate the whole thing for 2 hours @room temp. Then i've analyze it with MS..

Indeed i've found some BOC-Lysines and some Peptides which are BOC-protected @ N-Terminus.

Now here comes the question:

Do you think that there is a chance to bocylate ALL Lysines ?
( If not please tell me why..)

My consideration is to add more/higher concentration of BOC or more BASE (DIPEA)...or longer incubation time

Greets,
Diablooo

[Dan]

On paper, yes you should be able to BOC all the lysines side chains.

I suppose that if your peptide fragments are long enough to have well defined secondary/tertiary structure then some of the lysine side chains may be vey hindered. I don't know about that though, biochemistry is not my forte, it's just a thought.