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Bridge-IF: Learning Inverse Protein Folding with Markov Bridges

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arxiv 2411.02120 v1 pith:6C6XDEDQ submitted 2024-11-04 cs.LG cs.AIq-bio.BM

classification cs.LGcs.AIq-bio.BM
keywords proteinbridge-ifbridgedesignmarkovsequencesfoldinginverse
verification ladder T0 review T1 audit T2 compute T3 formal
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Inverse protein folding is a fundamental task in computational protein design, which aims to design protein sequences that fold into the desired backbone structures. While the development of machine learning algorithms for this task has seen significant success, the prevailing approaches, which predominantly employ a discriminative formulation, frequently encounter the error accumulation issue and often fail to capture the extensive variety of plausible sequences. To fill these gaps, we propose Bridge-IF, a generative diffusion bridge model for inverse folding, which is designed to learn the probabilistic dependency between the distributions of backbone structures and protein sequences. Specifically, we harness an expressive structure encoder to propose a discrete, informative prior derived from structures, and establish a Markov bridge to connect this prior with native sequences. During the inference stage, Bridge-IF progressively refines the prior sequence, culminating in a more plausible design. Moreover, we introduce a reparameterization perspective on Markov bridge models, from which we derive a simplified loss function that facilitates more effective training. We also modulate protein language models (PLMs) with structural conditions to precisely approximate the Markov bridge process, thereby significantly enhancing generation performance while maintaining parameter-efficient training. Extensive experiments on well-established benchmarks demonstrate that Bridge-IF predominantly surpasses existing baselines in sequence recovery and excels in the design of plausible proteins with high foldability. The code is available at https://github.com/violet-sto/Bridge-IF.

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Cited by 2 Pith papers

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

  1. EnerBridge-DPO: Energy-Guided Protein Inverse Folding with Markov Bridges and Direct Preference Optimization

    cs.LG 2025-06 conditional novelty 5.0 of 10

    A Markov-bridge inverse folding model fine-tuned with energy-based preference pairs and an explicit ΔΔG loss designs lower-energy protein complex sequences while keeping sequence recovery close to state-of-the-art.

  2. Solving Inverse Problems via Diffusion-Based Priors: An Approximation-Free Ensemble Sampling Approach

    cs.LG 2025-06 conditional novelty 5.0 of 10

    A weighted-particle sampler evolves the posterior through the diffusion model's reverse dynamics, with theoretical error bounds and improved image reconstructions.

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