RFD4-Proteina Goes Beyond Canonical Amino Acids, Distinguishing Adjacent Histone Sites
AllThingsApx · x · 2026-10-22
RFD4-Proteina's capabilities extend past the canonical 20 amino acids: following earlier work on phosphotyrosine binders, the model now supports designing with phosphoserine and phosphothreonine.
The team demonstrated binders that distinguish the adjacent H3pS10 and H3pT11 sites on the histone H3 tail — showing generative protein design can precisely tackle post-translational modification recognition, a notable AI4Science advance.
More from Research
- Interactive transformer diagrams now include backpropagation, aiming at model self-understanding — vtabbott_ · 2026-10-22
- Nankai and Alibaba propose PoS to break agents' 'Belief Trapping' — jiqizhixin · 2026-10-22
- Angler: A Tiny Sequence-to-Splicing Model That Runs on a Laptop and Beats Larger Models — anshulkundaje · 2026-10-22
- Chinese mathematician Sun Zhiwei proposes 1,000 problems to challenge AI — scmp_news · 2026-10-22
- Self-Amplifying RNA Programs Stem Cell Fate in One Transfection, Cell Reports Methods Paper Shows — anshulkundaje · 2026-10-22
- ETH Team Unveils 'Recordanelle', a Synthetic Organelle That Records Cell History in Nature Biotech — anshulkundaje · 2026-10-22