Insulin consists of two peptide chains, a shorter A-chain and a longer B-chain. The two chains are held together with disulfide bonds. Invivo, insulin is processed from a single polypeptide chain called proinsulin by specific protease. Processing involves removal of the C-chain from proinsulin as indicated.
A denaturation/renaturation experiment, similar to the one carried out by Anfinsen on ribonuclease, was performed. In contrast to his results, less than 10% activity was recovered upon removal of 2-Mercapoethanol and Urea. When the experiment was repeated on proinsulin , full activity was restored.
Please explain why this took place. A diagram is attached.© BrainMass Inc. brainmass.com October 16, 2018, 12:21 pm ad1c9bdddf - https://brainmass.com/biology/cell-biochem/activity-recovered-in-denaturing-renaturing-types-of-insulin-36152
In Anfinsen's original experiment, he denatured ribonuclease with 8M urea (this is a dissociating solvent and breaks all weak bonds). 2-mercaptoethanol is a reducing agent and reduces disulphide bridges to SH groups (sulphydryl), thus breaking them. This converts the enzyme to a random ...
The solution provides a few paragraphs' written explanation as to the results of a denaturation/renaturation experiment similar to that performed by Anfinsen on ribonuclease which were substantially different than expected.