I am so excited to share our new findings with you! We provide the structural evidence for a direct protein-to-DNA information pathway, showing how a bacterial enzyme 'reads' its own structure to 'write' DNA. www.science.org/doi/10.1126/...

Some like it hot!

Now out in its final form! www.science.org/doi/10.1126/...

Ever wonder how IDRs and folded domains work together to control function? Using ubiquilins, multidomain proteins involved in protein degradation, we show in our new preprint that IDRs aren’t just linkers, but regulate ensemble and function. Read it here: doi.org/10.64898/202...

Super excited to finally see this out! Also, hornwort emojis need to be publicly available

I aspire to exude as much confidence as this little Kinesin protein strutting along a microtubule while hauling intracellular cargo.

Look at that little guy go! 🔬🧪

Regret to announce that we’ve reached Wrong Coat season. Every coat you wear from now til mid April will be The Wrong Coat for the weather

The chloroplast ionome shines light on the dynamics of organellar iron homeostasis Loss of chloroplast iron (Fe) ferritin storage leads to Fe re-shuttling into the vacuole and reduced leaf tissue Fe content.

The chloroplast ionome shines light on the dynamics of organellar iron homeostasis academic.oup.com/plcell/artic... @theplantcell.bsky.social

A dynamic displacement mechanism drives protein import into mitochondria Most mitochondrial proteins are produced in the cytosol and imported through the translocase of the outer mitochondrial membrane (TOM) to reach their final destination. Although this protein entry gat...

📢 New preprint alert!
How do proteins enter mitochondria? We uncovered a surprising mechanism at the mitochondrial entry gate—using #NMR, in vivo single-particle tracking, yeast experiments, and MD simulations to crack the code.
www.biorxiv.org/content/10.6...
#StructuralBiology #Mitochondria
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How does protein folding change inside biomolecular condensates?

Our new preprint put forwards a framework for predicting this!! 🥳🥳🥳🥳 work by the talented @nathanieldhess.bsky.social

Every time people focus on resolution as a competitive number rather than what biochemical detailed is revealed at that resolution is being sent this little guy

"are you enjoying duo mobile" does a hamburger enjoy being made of quarks. does a fish enjoy linear time. does the mountain enjoy the first taste of a cup of hot chocolate when you get back to the ski lodge. your question means nothing to me. i couldn't enjoy duo mobile even if i tried

Crystallographic Ensembles Reveal the Structural Basis of Binding Entropy in SARS-CoV2 Macrodomain Structure-based drug design has traditionally focused on optimizing static, enthalpic interactions between ligands and proteins or on displacing binding site solvent molecules to entropically favor bi...

New preprint! Entropy drives molecular recognition, yet most structure-based drug design ignores it because it is difficult to measure. X-ray crystallography captures ensembles, not single structures. Can we extract thermodynamically meaningful entropy from them?

www.biorxiv.org/content/10.1...

CRISPR-Cas–mediated heritable chromosome fusions in Arabidopsis The genome of Arabidopsis thaliana consists of 10 chromosomes. By inducing CRISPR-Cas–mediated breaks at subcentromeric and subtelomeric sequences, we fused entire chromosome arms, obtaining two eight...

And now we have Arabidopsis plants with 8 chromosomes instead of 10 and no obvious phenotypic differences, this week in @science.org
#PlantScience
Paper here: www.science.org/doi/10.1126/...

Perspective here:
www.science.org/doi/10.1126/...

Rubisco is slow across the tree of life

@omc111.bsky.social

www.pnas.org/doi/10.1073/...

An illustration of a carbonic anhydrase complex in a synthetic mini-carboxysome

Pleased to see this collaboration with a great PhD student Pei Cing Ng, from Prof. Luning Liu's lab at Liverpool University published. Structure of the H. neapolitanus carbonic anhydrase and localisation in a mini-carboxysome: www.pnas.org/doi/epdf/10....

Every day I understand the Butlerian Jihad more and more

Global profiling of protein complex dynamics with an experimental library of protein interaction markers - Nature Biotechnology FLiP–MS uses a library of protein–protein interaction markers to understand protein complex dynamics.

FLiP–MS uses a library of protein–protein interaction markers to understand protein complex dynamics go.nature.com/4dQabQw
rdcu.be/eJI3A

Enzyme specificity prediction using cross attention graph neural networks - Nature Nature - Enzyme specificity prediction using cross attention graph neural networks

www.nature.com/articles/s41...

How does catalysis emerge from non-catalytic domains?

In our new paper, we show that catalytic activity can arise without conserved active-site residues — through multimerization and electrostatic features instead.

A striking case of catalysis evolving from binding.

This is super cool! I love the combination of computation and wet lab. The preference for slow codons in mitochondrial targeted proteins is thought provoking - presumably this could also be true of chloroplast targeted proteins

Awesome to see this epic piece of work, led by @cecclementi.bsky.social, finally appear in @natchem.nature.com.

The development of a general coarse-grained protein forcefield to describe folding, binding and conformation changes without solvent and all-atom, has been long anticipated!

Mapping allosteric rewiring in related protein structures from collections of crystallographic multiconformer models How do related proteins with a common fold perform diverse biological functions? Although the average structure may be similar, structural excursions from this average may differ, giving rise to allos...

New @biorxiv-biophys.bsky.social preprint from the #keedylab! 👀

www.biorxiv.org/content/10.1...

How do related proteins perform distinct functions despite sharing a similar structure?...

Working on modeling waters for the first time right now, currently leaning towards no, water is not real

I can’t wait for a coot-free future

Do structure, they said. It’ll be fun, they said. *quadsulfide bond appears*

Tennis Balls xkcd.com/3080

Advances in uncovering the mechanisms of macromolecular conformational entropy - Nature Chemical Biology Protein conformational entropy plays a vital role in functions like binding and catalysis. This Perspective discusses three ways macromolecules use conformational entropy: prepaying entropic costs, re...

A Perspective by @stephanieaw.bsky.social and @fraserlab.com discusses ways macromolecules use conformational entropy to control binding, catalysis, and allostery

www.nature.com/articles/s41...

A diagrame of the molecular parts used to make a synthetic biomolecular condensate and confocal microscopy images of the condensates

Outstanding work by @anyalb.bsky.social in my lab - she targeted enzymes to synthetic biomolecular condensates in plants and showed increases in metabolic pathway activity, likely due to protection of the introduced enzymes from proteolysis
#PlantScience
onlinelibrary.wiley.com/doi/10.1111/...

Protein function often depends on protein dynamics. To design proteins that function like natural ones, how do we predict their dynamics?

@hkws.bsky.social and I are thrilled to share the first big, experimental datasets on protein dynamics and our new model: Dyna-1!

🧵