Important FOLDING@HOME Update!!!!

Ecniv · 07-15-2003, 07:52 PM

I was browsing the www.littlewhitedog.com forums (I was a member of their team before I created the tech-forums team) And Fido (admin) just made this post, I think it is rather signifiant, and we may hear something very importatnt about this soon here is a quote from his post:

Quote:

QUICK! Someone fill the beer bowl!!!!

I've been doing some digging around to see what the **** has been going on with F@H lately (all teams stats have dropped considerably since 7/8/2003).

It turns out that a few of the NTL9 ("N-terminal domain of L9") projects have yeilded some "interesting results" which has warranted a massive immediate switch to nearly 100% deployment of p638_L939_K12M_ext & p639_L939_K12M_nat molecules.

Nobody is really saying what has been found at this point, but for them to basically turn off almost all other molecules and focus only on these types over and over again.... means someone has more than a hunch.

With that said... I don't mind the recent drop in stats due to the bombardment of p638_L939_K12M_ext & p639_L939_K12M_nat molecules.

It's all about the science boys and girls! Pass the bowl!!!

Find more info here.

Ecniv · 07-15-2003, 07:53 PM

Quote:

More info about NTL9....

Department of Chemistry, State University of New York at Stony Brook, Stony Brook, NY 11794-3400, USA.

The N-terminal domain of the ribosomal protein L9 forms a split betaalphabeta structure with a long C-terminal helix. The folding transitions of a 56 residue version of this protein have previously been characterized, here we report the results of a study of a truncation mutant corresponding to residues 1-51. The 51 residue protein adopts the same fold as the 56 residue protein as judged by CD and two-dimensional NMR, but it is less stable as judged by chemical and thermal denaturation experiments. Studies with synthetic peptides demonstrate that the C-terminal helix of the 51 residue version has very little propensity to fold in isolation in contrast to the C-terminal helix of the 56 residue variant. The folding rates of the two proteins, as measured by stopped-flow fluorescence, are essentially identical, indicating that formation of local structure in the C-terminal helix is not involved in the rate-limiting step of folding.