Sorry to go all AlphaFold-fanboy, but I have yet another example for you. This one requires a bit of back-story, so buckle in... I happen to be talking in the ACA meeting tomorrow, in Jane Richardson's session entitled "What Can & Can't We See Reliably at Resolution X?" (1/16)
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The rest was in entirely the wrong place, of course - unsurprising since its structure is completely controlled by interactions in the complex - but secondary structure (helix vs. coil) was correctly predicted. (12/16)
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About 20 minutes of refitting later... no real question that this is the right protein (allowing for a few point mutations given that it's the wrong species). (13/16)pic.twitter.com/CrL1VkKgTK
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Take-home messages: - it appears AlphaFold predictions are good enough to add a lot of confidence to sequence assignments even in the face of shallow alignments like this. (14/16)
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- it's quite spooky how easy it is when working without the benefit of a sequence to get something that looks kinda-sorta right while having the backbone backwards. (15/16)
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- *Don't* assume the genome database for your organism is complete! (Actually the second time this has come up for me - the first time the mystery chain was initially unidentified because its gene was missing from the mass spec database). (fin)
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End of conversation
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