Ivan Gushchin
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ivangushchin.bsky.social
Ivan Gushchin
@ivangushchin.bsky.social
Structural biology and protein engineering
"Study of the effect of acoustic treatment on freezing point and boiling point of tap water" - way to go for a scientific journal www.nature.com/articles/s41...
October 29, 2025 at 7:39 PM
October 16, 2025 at 7:28 PM
Previously, we engineered 3 artificial CagLOV-derived proteins doi.org/10.1002/pro.... - so I'm glad to see that the approach works for other LOVs as well
October 6, 2025 at 6:23 AM
They even succeed in engineering an ultrastable photoactive protein based on Atphot2 LOV2
October 6, 2025 at 6:23 AM
Interesting preprint by Herzog and colleagues where they investigate 21 diverse LOV domain - also beautiful illustrations throughout
October 6, 2025 at 6:23 AM
Glad to contribute to this: in our most recent preprint, we describe peculiar ferritin-like proteins that have ferroxidase activity, but do not form shells, using encapsulin compartments instead: doi.org/10.1101/2025...
October 1, 2025 at 7:36 PM
And now prohibitins!
www.pnas.org/doi/pdf/10.1...
September 27, 2025 at 8:05 PM
Got an idea while reviewing a grant and a paper

Image courtesy: Qwen
August 11, 2025 at 9:35 AM
Summer holidays @natcomms.nature.com ? 😕
July 21, 2025 at 3:10 PM
Great visual representation! Looks a little bit like a marketplace: choose the best organism for your specifications
July 20, 2025 at 9:55 AM
Interesting work from my former lab mate Vitaly Polovinkin and colleagues: solving a high resolution structure of a protein inside the cell using electron diffraction
July 12, 2025 at 12:08 PM
Happy to present a new flavin-binding protein that unexpectedly displays a large Stokes shift due to excited state proton transfer. Not submitted yet - feedback is welcome!

doi.org/10.1101/2025...
June 17, 2025 at 9:12 AM
Terrific work from Nikita Egorkin, Nikolai Sluchanko and their colleagues, who discovered a protein binding two carotenoids and two bilins (also four PC lipids!), thus mimicking absorption spectrum of green plants and giving crickets their color. Link to the PNAS article: doi.org/10.1073/pnas...
May 31, 2025 at 12:21 PM
It looks like Reviewer 1 was happy from the start, Reviewer 2 criticized crystallography and got the paper rejected, but said okay after revision. Still, this data collection and refinement statistics raises quite a number of questions.
May 15, 2025 at 7:36 AM
Having recently submitted manuscripts to Nature Communications/Science Advances and the like, very surprised to see the data like this published, claiming magnesium interaction. The purported resolution is 2.5 Å

doi.org/10.1038/s414...
May 15, 2025 at 7:32 AM
This literature/alphafold journey is inspired by Kirill's recent work on flotillin-associated non-rhodopsin (doi.org/10.1101/2025...) first found by Jose M. Haro-Moreno and colleagues (doi.org/10.1128/msys...). AlphaFold kind of sees some transmembrane interaction, but not particularly reliably
May 8, 2025 at 10:27 AM
Interestingly, E. coli flotillin homologue YqiK is so long that it cannot fit in the modeling box (do I understand that correctly?) and bent on itself. Moreover, AF3 is quite sure that it forms a complex with "Inner membrane protein YqiJ"
May 8, 2025 at 10:19 AM
Previous work on bacterial proteins HflK and HflC by Ma and colleagues is also beautiful: they even catch AAA+ proteases inside! This is likely needed to separate proteases from membrane proteins, as shown in the illustration

doi.org/10.1038/s414...
May 8, 2025 at 10:14 AM
Just learned that it turns out that flotillins form truncated cone-shaped compartments - beautiful structures from Fu and MacKinnon: doi.org/10.1073/pnas...
May 8, 2025 at 10:11 AM
Also, check out the map quality! Maybe we’ll get to individual protons one day
April 18, 2025 at 7:22 AM
Alternating access mechanism in proton-pumping microbial rhodopsin

Many thanks to everybody involved for the amazing data gathered over the years, and especially to Sergey for getting this over the finish line!

doi.org/10.1126/scia...
April 18, 2025 at 7:18 AM
I've tried modeling the effect of double Cys->Ser mutation, it changes the conformation of the sensor, but the transmembrane region remains the same. It is a well known problem of AlphaFold modeling that the conformations of different domains may not match.
March 22, 2025 at 10:17 AM
Great work! By the way, AlphaFold3 can make the model with better metrics and linked cysteines, although otherwise it looks very similar to yours. Prediction runs in ~10 minutes golgi.sandbox.google.com
March 22, 2025 at 10:12 AM
We used a related approach to predict stoichiometry of high-order circular homo-oligomers (ATPase c-rings), onlinelibrary.wiley.com/doi/full/10.... - although not so sophisticated, worked well on a test set including proteins, for which only AFM data is available
March 17, 2025 at 5:19 PM
We've tried this with spinach chloroplast ATPase rotor ring, which should be a tetradecamer (14-mer), and everything from 10 to 21 was modeled as a ring by AF2 doi.org/10.1002/prot...
January 26, 2025 at 11:11 PM