Pepsin not denatured at low pH?

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eaglflyrs@gmail.com - 28 Mar 2007 17:04 GMT

Hello, I was going over my notes for biochemistry and something struck
me. Somehow pepsin is not denatured at the low pH of the stomach while
many other proteins are, any idea why this is?

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MattLB - 29 Mar 2007 19:51 GMT

On Mar 28, 5:04 pm, eaglfl...@gmail.com wrote:

> Hello, I was going over my notes for biochemistry and something struck
> me. Somehow pepsin is not denatured at the low pH of the stomach while
> many other proteins are, any idea why this is?

Pepsin has three disulphide bridges that cross-link parts of the
polypeptide chain, which will assist in maintaining its shape in
otherwise denaturing conditions.

It may also not rely on positive/negative charge interactions (which
are affected by pH changes which add or remove positive hydrogen ions)
when folding up initially.

MattLB

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eaglflyrs@gmail.com - 30 Mar 2007 00:43 GMT

> On Mar 28, 5:04 pm, eaglfl...@gmail.com wrote:
>
[quoted text clipped - 11 lines]
>
> MattLB

Thank you!

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