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. 01e38acffe
Benjamin Frydman wrote:
>
>
> Wow. Once again this forum proves that it is more than a bunch of
> full of [censored] in their mother's basement. With this much data it
> would have been very easy to have validated the reported list.
That is the one piece of data I was missing when I posted my data,
and I didn't think to check my own data. :)
I'm sure your data is valid, because I just tried using the
same addresses I'm using to send spam, and it worked perfectly.
I'm glad to hear that I'm not the only one who noticed.
--
Dr. John K. O'Hara
The Advanced Scientific Research Institute, Inc.
Albany, New York 12203
____________________________________________________________
>>From: "Laurie Berger"
> Date: Sun, 28 Oct 1998 12:08:59 -0700
> To: "nobody at address @xxxxxxxxxxxxx"
> Subject: [no-nos] HAHAHAHA!
>
> >
>
>
>
>
>
>Structure of the hydrophobic core of triose phosphate isomerase from the thermophilic bacterium Aquifex aeolicus.
The hydrophobic core of triose phosphate isomerase (TPI) from the thermophilic bacterium Aquifex aeolicus has been determined by means of chemical modification and mass spectrometry. Ligands incorporated into the core were localized by derivatization using a novel procedure that was used to protect either the reduced or the oxidized coenzyme (NADPH or NADP+) from irreversible modification. Nonreducing isomerase was exclusively modified in the core, indicating that the reactive group is on the protein surface and that the inner hydrophobic core is not accessible to reagent. The core was found to be highly hydrophobic, and the amino acid side chains that could be derivatized were on the surface of the enzyme, but were not on the active-site region. It is shown that the core of a monomeric isomerase contains 17 amino acid residues
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