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ProtComposer: Compositional Protein Structure Generation with 3D Ellipsoids (2503.05025v1)

Published 6 Mar 2025 in q-bio.BM

Abstract: We develop ProtComposer to generate protein structures conditioned on spatial protein layouts that are specified via a set of 3D ellipsoids capturing substructure shapes and semantics. At inference time, we condition on ellipsoids that are hand-constructed, extracted from existing proteins, or from a statistical model, with each option unlocking new capabilities. Hand-specifying ellipsoids enables users to control the location, size, orientation, secondary structure, and approximate shape of protein substructures. Conditioning on ellipsoids of existing proteins enables redesigning their substructure's connectivity or editing substructure properties. By conditioning on novel and diverse ellipsoid layouts from a simple statistical model, we improve protein generation with expanded Pareto frontiers between designability, novelty, and diversity. Further, this enables sampling designable proteins with a helix-fraction that matches PDB proteins, unlike existing generative models that commonly oversample conceptually simple helix bundles. Code is available at https://github.com/NVlabs/protcomposer.

Summary

Analysis of "ProtComposer: Compositional Protein Structure Generation with 3D Ellipsoids"

The introduction of ProtComposer marks a significant advancement in the field of protein structure generation, addressing limitations in existing machine learning paradigms for protein design. Traditional methods have largely focused on unconditional generation or scaffold inpainting, lacking the ability to control complex protein spatial layouts. ProtComposer innovates by allowing users to specify a protein's spatial configuration using a set of 3D ellipsoids, providing a new avenue for controlled protein design.

The key methodology involves decomposing protein spatial layouts into modular components represented by these 3D ellipsoids. Each ellipsoid captures shape attributes and semantic annotations, such as secondary structure, and can be conditioned based on various sources: manually constructed layouts, extracted substructures from existing proteins, or novel configurations from a statistical model. This flexibility unlocks multiple capabilities, from redesigning protein connectivity to generating novel configurations that surpass existing designability, novelty, and diversity trade-offs.

Specifically, ProtComposer integrates an ellipsoid-based conditioning mechanism with the Multiflow model, a state-of-the-art joint sequence-structure flow-matching model. Multiflow is equipped with Invariant Point Attention, and ProtComposer introduces Invariant Cross Attention to facilitate an equivariant message passing between ellipsoids and residue frames. This innovative architecture enables fine-tuning the model to generate proteins that adhere closely to specified layouts while improving compositional complexity and secondary structure diversity.

Evaluation of ProtComposer reveals notable performance along several axes:

  1. Control: The model demonstrates strong adherence to conditioning layouts, yielding geometric and probabilistic alignment metrics that closely approach oracle-level outcomes derived from actual PDB proteins.
  2. Diversity and Novelty: By conditioning on synthetic ellipsoid layouts from a statistical model, ProtComposer significantly expands the diversity and novelty of generated proteins, achieving Pareto frontiers in these dimensions that are superior to existing multiflow variations.
  3. Compositionality: ProtComposer improves the architectural complexity of generated proteins, reducing the prevalence of oversimplified helix bundles typical of previous models.

The implications of ProtComposer are substantial in both practical and theoretical contexts. Practically, the ability to dictate precise protein layouts can revolutionize the design of biomolecular functions, offering a tool for researchers in protein engineering and synthetic biology. Theoretically, ProtComposer exemplifies the power of spatial conditioning in generative models, providing a framework that could be adapted to other domains where structural geometry is integral.

Speculative future applications within AI and protein design could see ProtComposer informing the generation of proteins with desired functionalities or interactions, potentially bridging the gap between structural biology and real-world protein applications. The model’s versatility in accepting various layout specifications opens new possibilities for creative protein design beyond the constraints of natural evolution, suggesting opportunities for innovations in drug design, enzymatic engineering, and beyond.

Overall, ProtComposer is a commendable advancement in computational biology, offering a robust, controllable, and diverse approach to protein structure generation. The paper embodies a significant step towards more intelligent, design-oriented protein engineering solutions.

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