[Protein-analysis] Re: Enthalpy of protein

Protenger via proteins%40net.bio.net (by yellowish from gmail.com)
Thu Mar 29 10:53:44 EST 2007


On Mar 29, 1:20 pm, Frank Küster <f... from kuesterei.ch> wrote:
> "Protenger" <yellow... from gmail.com> wrote:
> > I ask my question in another format.
> > Suppose we have a native protein with its own intristic (absolute)
> > enthalpy, then by protein engineering we introduce a pair
> > of opposide charged residues on its surface so its stability
> > increases.
> > Does absolut (and not delta H) enthalpy of mutant decrease?
>
> What is absolute enthalpy, and what is it good for to know it?
>
> Regards, Frank
> --
> But this:> For fucks sake...
>
> is just offensive.  It should have an apostrophe(!)
> [MJ Ray, nowhere]

One of my fellows said "by introducing stabilizing interaction in
proteins (in its core or surface) its enthalpy will increase"
This sentence have confused me very much, because as I have learned
before reactions (for example protein folding) tend to
reduce their enthalpy by releasing heat so stabilized protein (native)
relative to intermediate one (for example molten globule state) must
have a lower enthalpy.
So what about engineered proteins that stabilized for example by
introduced salt bridges?
What is the deference between intrinsic (absolute) enthalpy between
them?
Or clearly, which of them has higher enthalpy?

Regards, Rahim




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