Ox. reagent for proteins

Cornelius Krasel krasel at alf.biochem.mpg.de
Thu Dec 15 07:04:41 EST 1994


lw75 (Lynne_A_WHITEHEAD at UMAIL.UMD.EDU) wrote:
[...]

> There are essential disulfide bonds in my protein's
> structure for it's activity.  First, does anyone know why or what keeps
> disulfides from being formed in the cytoplasm (pH?, ect.)?

The cytoplasm is thought to be a reducing environment (the NADH : NAD ratio
is about 100:1 if I recall correctly) and there are indeed very few cyto-
plasmic proteins which possess disulfide bonds. The periplasm, on the
other hand, is thought to be an oxidizing environment, and if you manage
to export your protein, disulfide bonds will form rather easily.

The non-formation of disulfide bonds will not necessarily mean that
your protein does not have its native conformation, but it will quite
certainly be less stable.

--Cornelius.

--
/* Cornelius Krasel, Abt. Lohse, Genzentrum, D-82152 Martinsried, Germany  */
/* email: krasel at alf.biochem.mpg.de                 fax: +49 89 8578 3795  */
/* "Science is the game you play with God to find out what His rules are." */



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