After a couple of months puzzling and testing many design on boinc, a view small libraries of little miniproteins are ready to enter the lab. My structures are designed to mimic the well conserved catalytic core of the phospholipase membrane proteins and eventually bind organophosphorous compounds to neutralize the toxicity of those compounds.

Thanks to all participants of Rosetta@Home, I was able to run nearly 12'000 different designs in the last 9 weeks in a continuos optimization of design and forward folding. The calculations on boinc do not only tell if my design is the favorable state for the chosen sequence. After having visually inspected every individual forward folding plot (and I will for sure continue to do so), I do believe that the vast information content of every individual boinc calculation, is an important source of information to further understand the stabilizing features of proteins and eventually to define new design rules to more successfully guide our designs. Why? Because every individual boinc calculation is a very small piece of a big puzzle about the folding of proteins and is slightly different from any other boinc calculation, even if they do appear very similar.

Now that we have our first predicted libraries entering the lab state, we have a good starting point to create new optimized libraries, test them in the laboratory to give us more information on protein folding. My small protein scaffolds is just awesome for this purpose: their small size allows me to submit vast libraries of proteins onto boinc to obtain more accurate information. You can bet on one thing: I do intend to keep my pace on boinc in between the experiments to unravel the mystery around protein folding.

All out of a true passion and love for my small miniprotein. It's a passion because the miniproteins tell me so many stories. It's love for those miniproteins, because every miniprotein is an awesome unique individual with its own character.

Sincerely yours,
Ruud

Awesome - thanks for the update Ruud :D

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Thanks a lot for your post, continue your work and please keep us aware of your progress.

Hi, Ruud:


Many thanks for the information and best wishes for your continuing work.

John

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Encouraging results for the my first ever de novo designed proteins.

The far majority of proteins that I have selected using Rosetta@Home were expressed with very good yields and purity. With a very few exceptions, the proteins were obtained with a single band.

In addition, we have obtained encouraging results in a first attempt to bind organophosphate compounds. One of the proteins might have bound a fluorescent probe that serves as a template for OP-compounds. Currently, verification of this encouraging result is in progress.