charlesbj.bsky.social
Investigating protein nanomachines and their dynamics.
ARC DECRA Fellow at Monash University 🇦🇺.
Structural biologist. Author of WIGGLE. He/Him. 🏳️🌈
334 posts
1,325 followers
847 following
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throw*🤦♂️
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Ta! It really is the perfect summer dish 😍 Really tasty, not too heavy on a hot day, refreshing, and I don't feel guilty going back for more and more. It's also dead easy... Maybe a controversial opinion, but I quite like to through some bocconcini on top as well.
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Maybe Tillandsia recurvata? the flower is very cool!
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This one doesn’t look like much but it’s dCas9 Suntag labeling of a single gene where you can see both alleles moving in the nucleus of a live neuron 🤓
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I just finished admiring your work on the mitos... just incredible. Nice work mate :)
I am wondering about lysosomes and whether we can learn anything about the TOR pathway from this data... did you see many LROs?
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Very nice - I hoped this might happen. I notice MPNN struggles with particular targets. In these cases, as an alternative to avoid adversarial sequences, I've been screening relaxed trajectories with Boltz1 or chai1 to recover AF designed sequences that have <2 Å RMSD, low PAE etc. Any thoughts?
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Trying to guess your wall papers lol
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JWST?
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This has a nice summary... pubs.acs.org/doi/10.1021/...
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@lorneproteins.bsky.social 👀
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I told myself that I needed a large enough monitor to look at side chains within the whole complex... I might still need to get something bigger. 😅
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That will be super useful for small molecule compounds. Can it be extended? Constraining distances between protein chains alone is also very useful (eg when experimental distance constraints are known for a challenging complex).
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Awesome! I'll read up and give it a go. Any plans to implement additional experimental constraints, e.g. C alpha distances or cross-linking data (maybe already possible?).
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A class (average)
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And to you too! Your mTORC1 structure is beautiful 😍
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Thanks! Yes, certainly you could do it without the spheres, but you'd need a good color code. Personally for me the problem is seeing the magnitude. I find it quite difficult to look at colour alone and see the highly frequent mutations from the less frequent.
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Whoops! Still learning bsky. Forgot to say #cryoEM ;)
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Finally TSC is extraordinarily flexible and is a massively difficult structural biology target. We had to use all the tricks we know to get this one... Parts of TSC can move by up to 10 nm!!!
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Importantly, we discover that TSC recognises mono-phosphorylated phosphatidylinositols. These are known to regulate the mTORC1 pathway as signalling cues for growth.
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Our structure also highlights mutational hotspots, revealing new ways in which TSC mutations can drive disease or dysregulation of this pathway.
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We propose a docking mechanism that we expect is involved in TSC recruitment to the lysosomal membrane.
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TSC is conserved back to yeast and is the major regulator of the mTORC1 pathway. We combined protein crystallography, cryo-electron microscopy, cross-linking mass spectrometry, and bioinformatic analysis to obtain the most complete picture of TSC to date.
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This work was done at the Monash Biomedicine Discovery Institute. @MonashUni
Using our amazing @CryoEM_Monash facility. As always
Hari Venugopal is indispensible to our success!