pith. sign in

arxiv: 2507.09466 · v2 · pith:77O3GS52new · submitted 2025-07-13 · 💻 cs.LG · q-bio.QM

La-Proteina: Atomistic Protein Generation via Partially Latent Flow Matching

classification 💻 cs.LG q-bio.QM
keywords atomisticla-proteinaproteinlatentdesigngenerationmodelspartially
0
0 comments X
read the original abstract

Recently, many generative models for de novo protein structure design have emerged. Yet, only few tackle the difficult task of directly generating fully atomistic structures jointly with the underlying amino acid sequence. This is challenging, for instance, because the model must reason over side chains that change in length during generation. We introduce La-Proteina for atomistic protein design based on a novel partially latent protein representation: coarse backbone structure is modeled explicitly, while sequence and atomistic details are captured via per-residue latent variables of fixed dimensionality, thereby effectively side-stepping challenges of explicit side-chain representations. Flow matching in this partially latent space then models the joint distribution over sequences and full-atom structures. La-Proteina achieves state-of-the-art performance on multiple generation benchmarks, including all-atom co-designability, diversity, and structural validity, as confirmed through detailed structural analyses and evaluations. Notably, La-Proteina also surpasses previous models in atomistic motif scaffolding performance, unlocking critical atomistic structure-conditioned protein design tasks. Moreover, La-Proteina is able to generate co-designable proteins of up to 800 residues, a regime where most baselines collapse and fail to produce valid samples, demonstrating La-Proteina's scalability and robustness.

This paper has not been read by Pith yet.

discussion (0)

Sign in with ORCID, Apple, or X to comment. Anyone can read and Pith papers without signing in.

Forward citations

Cited by 6 Pith papers

Reviewed papers in the Pith corpus that reference this work. Sorted by Pith novelty score.

  1. A-CODE: Fully Atomic Protein Co-Design with Unified Multimodal Diffusion

    q-bio.QM 2026-05 unverdicted novelty 8.0

    A-CODE presents a fully atomic one-stage multimodal diffusion model for protein co-design that claims superior unconditional generation performance over prior one- and two-stage models plus a tenfold success-rate gain...

  2. Steerable Neural ODEs on Homogeneous Spaces

    cs.LG 2026-05 unverdicted novelty 7.0

    Steerable NODEs extend manifold neural ODEs by coupling base flow on homogeneous spaces with parallel transport of features in associated bundles, achieving G-equivariance under invariant conditions.

  3. General Multimodal Protein Design Enables DNA-Encoding of Chemistry

    cs.LG 2026-04 conditional novelty 7.0

    DISCO co-designs protein sequence and structure to produce functional heme enzymes that catalyze several new-to-nature carbene-transfer reactions at activities exceeding prior engineered enzymes.

  4. Coevolutionary Continuous Discrete Diffusion: Make Your Diffusion Language Model a Latent Reasoner

    cs.AI 2025-10 unverdicted novelty 7.0

    CCDD defines a joint multimodal diffusion on continuous representation space and discrete token space to combine expressivity with explicit token supervision for diffusion language models.

  5. Yeti: A compact protein structure tokenizer for reconstruction and multi-modal generation

    q-bio.BM 2026-05 unverdicted novelty 6.0

    Yeti is a compact tokenizer for protein structures that delivers strong codebook use, token diversity, and reconstruction while enabling from-scratch multimodal generation of plausible sequences and structures with 10...

  6. From Words to Amino Acids: Does the Curse of Depth Persist?

    cs.LG 2026-02 unverdicted novelty 6.0

    Protein language models exhibit consistent depth inefficiency where most task-relevant computation occurs in a subset of layers, mirroring patterns in large language models.