Deep learning-driven protein structure prediction and design: Key model developments by Nobel laureates and multi-domain applications
This systematic review outlines pivotal advancements in deep learning-driven protein structure prediction and design, focusing on four core models—AlphaFold, RoseTTAFold, RFDiffusion, and ProteinMPNN—developed by 2024 Nobel Laureates in Chemistry: David Baker, Demis Hassabis, and John Jumper. We analyze their technological iterations and collaborative design paradigms, emphasizing breakthroughs in atomic-level structural accuracy, functional protein engineering, and modeling multi-component biomolecular interactions. Key innovations include AlphaFold3's diffusion-based framework for unified biomolecular prediction, RoseTTAFold's three-track architecture integrating sequence and spatial constraints, RFDiffusion's denoising diffusion for de novo protein generation, and ProteinMPNN's inverse folding for sequence–structure co-optimization. Despite major progress in applications such as binder design, nanomaterials, and enzyme engineering, challenges persist in dynamic conformational sampling, multimodal data integration, and generalization to non-canonical targets. We propose future directions, including hybrid physics-AI frameworks and multimodal learning, to bridge gaps between computational design and functional validation in cellular environments.
Authors
- Yanwei Wang (ORCID: https://orcid.org/0009-0001-4725-0248)
- Yang Wang (ORCID: https://orcid.org/0000-0002-0092-927X)
- Wanqing Yang
Institutions
- Wenzhou University (CN)
Publication Details
- Journal
- Biophysics Reviews
- Published
- 2026-01-15
- DOI
- https://doi.org/10.1063/5.0273394
- Primary Topic
- Protein Structure and Dynamics
- Type
- article
- Field-Weighted Citation Impact
- 0.00