Question

1. Use your own words or drawing to show the protonation and deprotonation of Lysine when PH increase from 1 to 11.

2. We know that the pKa of Histidine is 6.5. Explain what will happen at physiological pH. And it is the residue most frequently involved in enzymemediated catalysis. Explain why base on the known features of Histidine. You can use serine protease Trypsin as an example.

These are my protein structure homework, pls help

Answer 1

Golden Rule If PH of solution is 2 units above Value o Deprotonated amino acid 2 IFpH of Soutn is 2 unts below the pKa PROTONATED FORM 's the Z㈧ITTER 10N exists So, frem pH,-(1 to 3-5) _ apply ule① depro to nated fo.am exists NH