Denaturation and refolding of an enzyme

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enzsel
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Denaturation and refolding of an enzyme

Post by enzsel » Thu Dec 02, 2010 1:54 pm

Q1.Lysozyme is a very stable protein with four disulphide bonds. How does this structural feature relate to its function?

I think the answer Lysozyme is a protein found in many human secretions, such as tears, milk, mucus and saliva.Lysozyme protects against bacterial infection by breaking down the carbohydrates in bacterial cell walls, killing them.
lysozyme retains the antibacterial activity and stabileses cross linkages. The presence of disulphide bonds make the protein less suspectible to unfolding when tHey leave the intracellular environment . Disulphide bonds act as ataomic stable to reinforce most favourite conformation and dont change the conformation of protein.
I have done research everywhere but dont get the question and not sure about the answer too, if i am exactly answering the question?

Q2.What is the function of cysteine in the renaturation reaction?
I think the answer : The side chain on cysteine is thiol participates in enzymatic reactions and act as nucleophile.
Cysteine residues play a valuable role by crosslinking proteins, which increases the rigidity of proteins and also functions to confer proteolytic resistance.

Can you help me please?

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JackBean
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Post by JackBean » Thu Dec 02, 2010 2:14 pm

Q1: well, you have answered, why is it so stable, but does that relate to its function?

Q2: I don't think the Cys-Cys bonds prevent proteolytic degradation (but I may be wrong), but otherwise it seems OK
http://www.biolib.cz/en/main/

Cis or trans? That's what matters.

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canalon
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Post by canalon » Thu Dec 02, 2010 2:21 pm

Q1 would agree with your answer. Stabilization of the secreted protein in varied environments.
Patrick

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any proof. (Ashley Montague)

enzsel
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Post by enzsel » Sat Dec 04, 2010 9:36 pm

thank you

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