Danny Diaz (@aiproteins) 's Twitter Profile
Danny Diaz

@aiproteins

Changing the World! One protein at a time! ML Protein Engineer | DeepProteins @MLFoundations | Entrepreneur

ID: 1005975495400411138

linkhttp://danny305.github.io calendar_today11-06-2018 00:50:23

644 Tweet

407 Followers

418 Following

Tony Kulesa (@kulesatony) 's Twitter Profile Photo

New review out today in Nature Biotech on nanopore-based protein sequencing. Feels... like... something... coming... soon... 👀

New review out today in Nature Biotech on nanopore-based protein sequencing. 

Feels... like... something... coming... soon... 👀
Eric Topol (@erictopol) 's Twitter Profile Photo

Of >105,000 participants with 30-year follow-up, only 9.3% achieved healthy aging (age 70, w/o any chronic diseases). Their diet was significantly associated with this outcome🧵 Nature Medicine

Of &gt;105,000 participants with 30-year follow-up, only 9.3% achieved healthy aging (age 70, w/o any chronic diseases). Their diet was significantly associated with this outcome🧵 <a href="/NatureMedicine/">Nature Medicine</a>
Gabriel Rocklin (@grocklin) 's Twitter Profile Photo

Small proteins can be more complex than they look! We know proteins fluctuate between different conformations- but how much? How does it vary protein to protein? Can highly stable domains have low stability segments? Állan Ferrari experimentally tested >5,000 domains to find out!

Small proteins can be more complex than they look!

We know proteins fluctuate between different conformations- but how much? How does it vary protein to protein? Can highly stable domains have low stability segments? <a href="/ajrferrari/">Állan Ferrari</a> experimentally tested &gt;5,000 domains to find out!
Pranam Chatterjee (@pranamanam) 's Twitter Profile Photo

Our pLM-designed peptides, when attached to E3 ligases (aka uAbs), enable us to programmably degrade disease targets (think CRISPRi, but for proteins). But what if we want to STABILIZE useful proteins? In Nature Communications, we introduce duAbs! 🌟 📜: nature.com/articles/s4146… 🧬:

Our pLM-designed peptides, when attached to E3 ligases (aka uAbs), enable us to programmably degrade disease targets (think CRISPRi, but for proteins). But what if we want to STABILIZE useful proteins? In <a href="/NatureComms/">Nature Communications</a>, we introduce duAbs! 🌟  

📜: nature.com/articles/s4146…
🧬:
Jude Wells (@_judewells) 's Twitter Profile Photo

I really like this ProGen3 paper because, contrary to the title, I think it actually shows there is relatively little to be gained from massively scaling protein language models. 1/n

I really like this ProGen3 paper because, contrary to the title, I think it actually shows there is relatively little to be gained from massively scaling protein language models. 1/n
Danny Diaz (@aiproteins) 's Twitter Profile Photo

Has anyone else noticed that the quality of ChatGPT has gone down significantly recently? Spend more time correcting it than using it. OpenAI I need my money back.

Kyle Tretina, Ph.D. (@allthingsapx) 's Twitter Profile Photo

Read more: Predicting pose distribution of protein domains connected by flexible linkers is an unsolved problem biorxiv.org/content/10.110…

Alec Helbling (@alec_helbling) 's Twitter Profile Photo

Flow matching produces smooth, deterministic trajectories. In contrast, the sampling process of a diffusion model is chaotic, resembling the random motion of gas particles.

jack morris (@jxmnop) 's Twitter Profile Photo

new paper from our work at Meta! **GPT-style language models memorize 3.6 bits per param** we compute capacity by measuring total bits memorized, using some theory from Shannon (1953) shockingly, the memorization-datasize curves look like this: ___________ / / (🧵)

new paper from our work at Meta!

**GPT-style language models memorize 3.6 bits per param**

we compute capacity by measuring total bits memorized, using some theory from Shannon (1953)

shockingly, the memorization-datasize curves look like this:
      ___________
  /
/

(🧵)
Danny Diaz (@aiproteins) 's Twitter Profile Photo

A really great case study on how everyone wants to train flashy deep learning models but nobody wants to spend the time cleaning/curating the datasets and inspecting the quality of model predictions. This is very prevalent in protein AI research. rachel.fast.ai/posts/2025-06-…

Biology+AI Daily (@biologyaidaily) 's Twitter Profile Photo

Gaia: An AI-enabled genomic context–aware platform for protein sequence annotation Science Advances 1.Gaia introduces a new paradigm in protein function annotation by combining sequence, structural, and crucially, genomic context information into a unified, scalable search

Gaia: An AI-enabled genomic context–aware platform for protein sequence annotation <a href="/ScienceAdvances/">Science Advances</a>

1.Gaia introduces a new paradigm in protein function annotation by combining sequence, structural, and crucially, genomic context information into a unified, scalable search
Danny Diaz (@aiproteins) 's Twitter Profile Photo

It is imperative that we continue to fund CASP and other similar competitions that fuel innovation in computational protein science and underpin future biotechnology innovations. Please share and reach out to your congress representatives! #FundCASP science.org/content/articl…

Biology+AI Daily (@biologyaidaily) 's Twitter Profile Photo

Ambient Proteins: Training Diffusion Models on Low Quality Structures 1. A new framework, Ambient Protein Diffusion, revolutionizes protein structure generation by leveraging low-confidence AlphaFold structures as valuable, corrupted training data instead of discarding them.

Ambient Proteins: Training Diffusion Models on Low Quality Structures

1.  A new framework, Ambient Protein Diffusion, revolutionizes protein structure generation by leveraging low-confidence AlphaFold structures as valuable, corrupted training data instead of discarding them.
Kyle Tretina, Ph.D. (@allthingsapx) 's Twitter Profile Photo

AI just shrank evolutionary analysis from hours → heartbeats🧬 SelRegAA transformer classifies evo selection for amino‑acid sites ≈1,000× faster than codeml ⚡️ DL models are replacing classical likelihood methods in molecular evolution 😅

AI just shrank evolutionary analysis from hours → heartbeats🧬

SelRegAA transformer classifies evo selection for amino‑acid sites ≈1,000× faster than codeml ⚡️

DL models are replacing classical likelihood methods in molecular evolution 😅
Danny Diaz (@aiproteins) 's Twitter Profile Photo

Had a lot of fun learning diffusion and addressing key issues in protein diffusion with Giannis Daras Jeffrey Ouyang-Zhang TLDR: a few protein structure insights inspired us to design a new diffusion loss, training regime and dataset, resulting in significant performance improvements

Pranam Chatterjee (@pranamanam) 's Twitter Profile Photo

Toxic heavy metals contaminate ecosystems and harm vulnerable communities. 🌎⚠️ Here, we present Metalorian, a conditional diffusion model that generates heavy metal-binding peptides, validated by MD and experiments! 💻🧪 📜: biorxiv.org/content/10.110… 🤗: huggingface.co/ChatterjeeLab/…

Toxic heavy metals contaminate ecosystems and harm vulnerable communities. 🌎⚠️ Here, we present Metalorian, a conditional diffusion model that generates heavy metal-binding peptides, validated by MD and experiments! 💻🧪

📜: biorxiv.org/content/10.110…
🤗: huggingface.co/ChatterjeeLab/…
Danny Diaz (@aiproteins) 's Twitter Profile Photo

Turns out using co-pilot/AI during software development actually slows down productivity in a randomized clinical trial sitting. 🤔 metr.org/blog/2025-07-1… Personally, it saves me a lot of time when writing data analysis code, or refactoring bad code. What do y’all think?

Biology+AI Daily (@biologyaidaily) 's Twitter Profile Photo

AlphaFlex: Accuracy Modeling Of Protein Multiple Conformations Via Predicted Flexible Residues A new computational framework, AlphaFlex, has been introduced to address the long-standing challenge of accurately and efficiently modeling multiple protein conformational states, a

AlphaFlex: Accuracy Modeling Of Protein Multiple Conformations Via Predicted Flexible Residues

A new computational framework, AlphaFlex, has been introduced to address the long-standing challenge of accurately and efficiently modeling multiple protein conformational states, a