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Google's DeepMind Predicts 3D Shapes of Proteins (theguardian.com) 51

Google's DeepMind is using an AI program, called AlphaFold, to predict the 3D shapes of proteins, the fundamental molecules of life. "DeepMind set its sights on protein folding after its AlphaGo program famously beat Lee Sedol, a champion Go player, in 2016," reports The Guardian. The company says "It's never been about cracking Go or Atari, it's about developing algorithms for problems exactly like protein folding." From the report: DeepMind entered AlphaFold into the Critical Assessment of Structure Prediction (CASP) competition, a biannual protein-folding olympics that attracts research groups from around the world. The aim of the competition is to predict the structures of proteins from lists of their amino acids which are sent to teams every few days over several months. The structures of these proteins have recently been cracked by laborious and costly traditional methods, but not made public. The team that submits the most accurate predictions wins. On its first foray into the competition, AlphaFold topped a table of 98 entrants, predicting the most accurate structure for 25 out of 43 proteins, compared with three out of 43 for the second placed team in the same category.

To build AlphaFold, DeepMind trained a neural network on thousands of known proteins until it could predict 3D structures from amino acids alone. Given a new protein to work on, AlphaFold uses the neural network to predict the distances between pairs of amino acids, and the angles between the chemical bonds that connect them. In a second step, AlphaFold tweaks the draft structure to find the most energy-efficient arrangement. The program took a fortnight to predict its first protein structures, but now rattles them out in a couple of hours.

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Google's DeepMind Predicts 3D Shapes of Proteins

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  • They took our jobs! (Score:3, Interesting)

    by Anonymous Coward on Tuesday December 04, 2018 @04:25AM (#57745988)

    DeepMind is moving out of the realm of curiosity (games) to things that employ people with a high degree of specialization. Google's team of 10 people produced a better result with 2 years of work than the entire academic field has been able to produce in the last 30. Granted, they had prior work to inform them. Anyway, this is interesting because this kind of development can put the PhD's in my lab out of a job - and they thought the truck drivers would be first to get automated!

    • That's a ridiculous position to take, science is about working on things we are somewhat aware of, but don't quite yet understand properly. And every question you answer opens up ten new ones. Nobody cracks protein structures for the sake of cracking protein structures, these problems are solved because they are prerequisites to solving other problems. Like looking for an Alzheimer cure etc. It's not about solving the riddle, it's about things you can do once you have solved the riddle.
    • Yeah, no. Protein folding computer programs have been around for years. It wasn't done by hand. More hype from the AI nutters.
      • Well no, it's not hype. They aced the competition by a good margin, clearly they are doing something right. It's not like the other competitors are solving these problems manually.
      • Come on, you can do better than this. I finally looked you up and you got 2^8 +5 comments. You can do much better than this. Why obsess with AI nutters, space idiots and Tesla fanbois?

        Who is a bigger idiot, these nutjobs or the one with the mission to correct every nutjob on the net? Just chill. Why waste good time chasing these nutjobs.

        Best of luck buddy.

      • The method they used only works when there are a gazillion similar sequences. It doesn't work for a unique sequence. So it's not an "ab initio" method, it's a fold recognition method done by recognizing the contacts then free form folding to fit that. But it can't infer contacts without massive sequence alignments to other proteins. Thus it has great value in those cases but other methods work in all cases not just that special case.

    • You think that's bad? Radiologists are already significantly better with AI and give it a few more iterations and you'll only need a few of the best radiologists to handle the edge cases, then it's all machine learning on outliers.

      Sorry about that fellowship you did - back to primary care with you - don't forget to swap out that BMW for a Prius.

      • by ceoyoyo ( 59147 )

        More like swap out that Maserati for a BMW. The primary care types do pretty well too, but it's hard to match the throughput of a good radiologist.

        Problem with the primary care physicians is that the part of their job that's not vulnerable to machine learning is done better by nurses. Surgeons should have job security for a while.

    • Google's team of 10 people produced a better result with 2 years of work than the entire academic field has been able to produce in the last 30

      That's not a correct reading of the results. First, previous efforts are based on putative understanding about how proteins fold. Obviously, this understanding is incomplete - or the physics based methods would perform better. (Even statistical potentials like in Rosetta are physics based in important ways). Second, DeepMind isn't even on the radar in the server component of CASP. The server competition is intrinsically more difficult because it requires robust software that isn't highly dependent on user p

  • I'm looking forward to the research paper to address key questions. What resources (training, inference) did Google use and how do they compare to the competition? Was this mostly a machine learning problem with big data, or a big data problem with some machine learning? Is there a GitHub yet?

    • by MrMr ( 219533 )
      Normally the CASP proceedings appear more than a year after the meeting. There is some info on their own website: https://deepmind.com/blog/alph... [deepmind.com]
      An interesting question is the claim that they generate shapes ab initio, but using a neural network. I wonder how much the network has been trained to recognize existing (evolutionary dependent) protein families and their patterns vs. a new random sequence folder. The former may be just as useful in practice but may teach us a bit less about the mechanics of f
      • I wonder how much the network has been trained to recognize existing (evolutionary dependent) protein families and their patterns vs. a new random sequence folder.

        That's why they should use the historical validation approach! Train on structures solved before 2005, then predict only novel folds solved after 2005. Perform well in that context and I'll be impressed.

        The former may be just as useful in practice but may teach us a bit less about the mechanics of folding.

        Unlike the physics-based and statistical potential methods, can the DeepMind approach ever contribute to understanding how proteins fold? IMHO that's an open question, and one that's critical to their presumably forthcoming publication. For example, do their features weights say something interesting about c

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