AlphaFold solved the protein folding problem some time ago and now, judging from two articles in today's issue of the journal Science, it looks like the inverse problem has also been solved, the protein design problem. If you tell a program called "ProteinMPNN" that you want a 3-D protein that has an activation site that will perform a very specific function, and has the proper scaffolding to keep that activation site stable, and is also shaped in just the right way so that it can fit into a very tight corner where it is needed like a key into a lock, then ProteinMPNN will tell you what linear sequence of amino acids will fold up into that 3-D shape. I think this is a very big deal, the implications for medicine are obvious but it also signifies a huge advance in Nanotechnology because the authors claim the 3-D shape the sequence of amino acids folds up into is within 0.06 Nanometers of the requested shape, and Nanotechnology is about placing atoms exactly where you want them to go, and enzymes are proteins and they act like little machines.
Robust deep learning–based protein sequence design using ProteinMPNN <https://www.science.org/doi/10.1126/science.add2187> Hallucinating symmetric protein assemblies <https://www.science.org/doi/10.1126/science.add1964> John K Clark -- You received this message because you are subscribed to the Google Groups "Everything List" group. To unsubscribe from this group and stop receiving emails from it, send an email to everything-list+unsubscr...@googlegroups.com. To view this discussion on the web visit https://groups.google.com/d/msgid/everything-list/CAJPayv2kQNjwf6pB-uxG1TDoGbMy8orDMOXKq%3DiXyzEhB%3DADXQ%40mail.gmail.com.
