REVIEW 4 cited by
Protein Conformation Generation via Force-Guided SE(3) Diffusion Models
Not yet reviewed by Pith; the record is open.
This paper has not been read by Pith yet. Machine review is queued; the pith claim, tier, and objections will appear here once it completes.
SPECIMEN: schema-true, not a live event
T0 review · schema-true
One-sentence machine reading of the paper's core claim.
pith:XXXXXXXX · record.json · timestamp
Signed reviews
read the original abstract
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.
Forward citations
Cited by 4 Pith papers
-
FlowBack-Adjoint: Physics-Aware and Energy-Guided Conditional Flow-Matching for All-Atom Protein Backmapping
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.
-
Generative Modeling of Full-Atom Protein Conformations using Latent Diffusion on Graph Embeddings
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.
-
Aligning Protein Conformation Ensemble Generation with Physical Feedback
EBA fine-tunes a protein diffusion model by reweighting sampled conformations according to their force-field energies, improving ensemble realism on the ATLAS benchmark.
-
ProtPainter: Draw or Drag Protein via Topology-guided Diffusion
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.
Discussion (0). Continue with ORCID to comment.