Yeah, I tried to really simplfy it, as it had been first explained to me
when I first got interested in these beasties in my oceanography class,
some 3 years ago.
>
> > >springiness to it to stay in solution, and must be able to be broken
> > >apart with little energy input. Too much energy input, and the molecule
> > >will break apart and precipitate out of solution, which is how egg
>
> Well, it is not "breaking", it is a simple, sharp phase transition from
> the precisely defined point in state (=conformation space, form follows
> function (aka mapping (folding) of a linear polymer (string), a
> precisely defined, intricate 3-shape, which maps to the task space of
> that particular protein in a wet context)) to a wide variety (a very
> large region of energetically accessible state space) of denaturated
> structures.
I love it when I get someone going in their own wave.
>
> > >whites get white when you boil them. Using different elements at the
> > >energy bond points than is used for normal temp organisms allows for
> > >much higher temperature tolerance, as the bonds are much tighter, and
>
> I can assure you, extreme thermophiles bugs use exactly the same amino
> acids as the rest of us, just in a different sequence. A single point
> mutation can increase the stability of a protein dramatically.
>
> > >require higher energy input to break them apart, however this makes for
> > >a very tightly bound molecule that only does its chemical work at a
> > >higher temperature. For example, a common protein in bacteria which uses
> > >iron in its makeup, has a corollary protein in hyperthermophilic
> > >bacteria (bacteria that can live above boiling) that uses tungsten
> > >instead.
>
> Ok, so you're refering to the cofactors. But this is fringe adaptation,
> the rest of the beastie is still conventional. (You're not referring ;)
> to Cytochrome C, do you? Do they actually use tungsten instead of iron?)
As I recall, it was an archae type, although I could be mistaken.
Mike