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This is our software to help you build your own novel synthetic proteins if you want to give it a try yourself right now in your browser (built with Go and Embe
by jfarlow 10y ago
This is our software to help you build your own novel synthetic proteins if you want to give it a try yourself right now in your browser (built with Go and Ember!):
https://serotiny.bio/ https://serotiny.bio/
No knowledge of DNA or cloning techniques are needed to use it. Drag and drop protein domains with the functions you want to produce a single protein with those functions. And if you wish, we can help place the order for your design with a DNA synthesizer so that the DNA that encodes your new protein arrive in the mail. Entire companies are founded on single good ideas for how to assemble these protein parts. Come up with your own.
It's also a great place to learn about how others are designing their synthetic proteins. The intent is to build up a plain language app-store for all of these various capabilities, as well as keep track of how the various proteins get used. At the end of the day it's not the DNA that does anything in an organism, it's the proteins that are really the machines of your body. If the DNA is the source code, the proteins are the apps themselves. DNA is cool and philosophical, but proteins are useful.
Here is a list and short description of proteins as they've come up on HN in the past few months. I've been trying to keep a list of 'proteins of interest' that have some social, economic, or medical interest to Hacker News:
https://serotiny.bio/notes/proteins/ https://serotiny.bio/notes/proteins/
- kanzure 10y agoHow often do fusion proteins fail to work? I see a lot of "just stick this catalytic domain to dCas9" and I am not really sure why that works.
- jfarlow 10y agoMore times than not protein fusions work just fine for the desired definition of 'work'. If you are trying to tune the very last efficiency out of an enzyme, or push one organism's survival efficiency past another's, then yeah smashing domains together is not the way you arrive at an evolutionarily polished machine. However if you need to test or create new functionality it seems to work just fine. Biology is extraordinarily robust. A common technique is to combine these to approaches - build out a rationally designed functional protein by fusion, then run it through a few rounds of directed evolution to have the organisms themselves iron out the kinks. This strategy has been very successful. Just smashing GFP onto every protein in the yeast proteome resulted in ~80% successfully turning green without noticeably affecting the yeast growth.[1] Check out eCD4-IG - it's four components fused to become an extraordinarily effective anti-HIV drug. It is of a different kind and a different order of effectiveness then the small molecule drugs of the 20th century.[2] [1] http://www.nature.com/nature/journal/v425/n6959/full/nature02046.html http://www.nature.com/nature/journal/v425/n6959/full/nature0... [2] https://serotiny.bio/notes/proteins/ecd4ig/ https://serotiny.bio/notes/proteins/ecd4ig/