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Protein Conformation Generation via Force-Guided SE(3) Diffusion Models

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arxiv 2403.14088 v2 pith:O4624H77 submitted 2024-03-21 q-bio.BM cs.LG

classification q-bio.BMcs.LG
keywords proteindiffusionconformationconformationsforce-guidedgenerationmodelsconfdiff
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The conformational landscape of proteins is crucial to understanding their functionality in complex biological processes. Traditional physics-based computational methods, such as molecular dynamics (MD) simulations, suffer from rare event sampling and long equilibration time problems, hindering their applications in general protein systems. Recently, deep generative modeling techniques, especially diffusion models, have been employed to generate novel protein conformations. However, existing score-based diffusion methods cannot properly incorporate important physical prior knowledge to guide the generation process, causing large deviations in the sampled protein conformations from the equilibrium distribution. In this paper, to overcome these limitations, we propose a force-guided SE(3) diffusion model, ConfDiff, for protein conformation generation. By incorporating a force-guided network with a mixture of data-based score models, ConfDiff can generate protein conformations with rich diversity while preserving high fidelity. Experiments on a variety of protein conformation prediction tasks, including 12 fast-folding proteins and the Bovine Pancreatic Trypsin Inhibitor (BPTI), demonstrate that our method surpasses the state-of-the-art method.

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Forward citations

Cited by 4 Pith papers

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

  1. FlowBack-Adjoint: Physics-Aware and Energy-Guided Conditional Flow-Matching for All-Atom Protein Backmapping

    physics.chem-ph 2025-08 conditional novelty 6.0 of 10

    FlowBack-Adjoint fine-tunes a flow-matching backmapping model with molecular mechanics energy gradients, reducing clashes and bond errors and producing lower-energy all-atom protein reconstructions.

  2. Generative Modeling of Full-Atom Protein Conformations using Latent Diffusion on Graph Embeddings

    q-bio.BM 2025-06 conditional novelty 6.0 of 10

    LD-FPG generates all-atom conformations of the D2 dopamine receptor from a latent diffusion model trained on MD snapshots, reaching all-atom lDDT around 0.7 and low dihedral-angle divergence.

  3. Aligning Protein Conformation Ensemble Generation with Physical Feedback

    q-bio.BM 2025-05 conditional novelty 6.0 of 10

    EBA fine-tunes a protein diffusion model by reweighting sampled conformations according to their force-field energies, improving ensemble realism on the ATLAS benchmark.

  4. ProtPainter: Draw or Drag Protein via Topology-guided Diffusion

    cs.AI 2025-04 conditional novelty 6.0 of 10

    Protein backbones can be generated or edited by drawing 3D curves, through a two-stage pipeline that predicts secondary structure from the curve and guides denoising diffusion sampling.

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