Question

You have a protein with a sulfhydryl group (S-H) how could you use that to isolate your protein?

Another option would be to use a 6X histidine linker. How would that work?

Would one have an advantage over the other?

Answer 1

• Sulfhydril in protein cures wound healing and found the protein functionality and also impotant role in food digestion.

The S-H bond isolates the S-S bond.Sulphyl hydrides present in proteins but not more an primary amines.

The S-S bonds in protein they block the binding sites. The S-H bond is used to isolate these S-S bond.

The formation of Thio ether bond Sulfhydril is used.

• In proteins the hystidine bonds are used to recomibinent proteins.

This results pure protein in prokaryotic organisms.

This Hystidine only involves in primary structure of proteins.

It is also used in the secondary chromatographic technique for the eliminates impurities.

Advantages:

Histadine stabilises higher P^H.   

Histadine immobilize the protein.

The S-H group is used to find cellular respiration in the rearly stage.

The free S-H group in insuline coinsides loss in activity.