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[return to "AlphaFold reveals the structure of the protein universe"]
1. COGlor+JD[view] [source] 2022-07-28 15:03:35
>>MindGo+(OP)
Before my comment gets dismissed, I will disclaim I am a professional structural biologist that works in this field every day.

These threads are always the same: lots of comments about protein folding, how amazing DeepMind is, how AlphaFold is a success story, how it has flipped an entire field on it's head, etc. The language from Google is so deceptive about what they've actually done, I think it's actually intentionally disingenuous.

At the end of the day, AlphaFold is amazing homology modeling. I love it, I think it's an awesome application of machine learning, and I use it frequently. But it's doing the same thing we've been doing for 2 decades: pattern matching sequences of proteins with unknown structure to sequences of proteins with known structure, and about 2x as well as we used to be able to.

That's extremely useful, but it's not knowledge of protein folding. It can't predict a fold de novo, it can't predict folds that haven't been seen (EDIT: this is maybe not strictly true, depending on how you slice it), it fails in a number of edge cases (remember, in biology, edge cases are everything) and again, I can't stress this enough, we have no new information on how proteins fold. We know all the information (most of at least) for a proteins final fold is in the sequence. But we don't know much about the in-between.

I like AlphaFold, it's convenient and I use it (although for anything serious or anything interacting with anything else, I still need a real structure), but I feel as though it has been intentionally and deceptively oversold. There are 3-4 other deep learning projects I think have had a much greater impact on my field.

EDIT: See below: https://news.ycombinator.com/item?id=32265662 for information on predicting new folds.

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2. ramraj+oJ[view] [source] 2022-07-28 15:29:00
>>COGlor+JD
Not sure if you should be reminded of how alpha fold started, it started by winning a competition thought un winnable by academics. Top labs working in protein structure prediction have fundamentally changed direction after alpha fold and are working to do the same even better.

This is not the first (or even tenth) time I’m seeing an academic trying to undermine genuine progress almost to the level of gaslighting. Comparing alphafold to conventional homology modeling is disingenuous at its most charitable interpretation.

Not sure what else to say. Structural biology has always been the weirdest field I’ve seen, the way students are abused (crystallize and publish in nature or go bust), and how every nature issue will have three structure papers as if that cures cancer every day. I suppose it warps one’s perception of outsiders after being in such a bubble?

signed, someone with a PhD in biomedical engineering, did a ton of bio work.

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3. shpong+MO[view] [source] 2022-07-28 15:52:00
>>ramraj+oJ
> Comparing alphafold to conventional homology modeling is disingenuous at its most charitable interpretation.

It's really not - have you played around with AF at all? Made mutations to protein structures and asked it to model them? Go look up the crystal structures for important proteins like FOXA1 [1], AR [2], EWSR1 [3], etc (i.e. pretty much any protein target we really care about and haven't previously solved) and tell me with a straight face that AF has "solved" protein folding - it's just a fancy language model that's pattern matching to things it's already seen solved before.

signed, someone with a PhD in biochemistry.

[1] https://alphafold.ebi.ac.uk/entry/P55317 [2] https://alphafold.ebi.ac.uk/entry/P10275 [3] https://alphafold.ebi.ac.uk/entry/Q01844

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4. ramraj+sk1[view] [source] 2022-07-28 17:58:08
>>shpong+MO
I can see the loops in these structures. I dont see the problem. It still added a structure to every embl page, and people are free to judge the predictions themselves. For all I care (ostensibly as the end customer of these structures) I don’t mind having a low confidence structure for any arbitrary protein at all. It’s only marginally less useful to actual biology than full on X-ray structures anyway.
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