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Diffusion probabilistic models enhance variational autoencoder for crystal structure generative modeling.

ABSTRACT: The crystal diffusion variational autoencoder (CDVAE) is a machine learning model that leverages score matching to generate realistic crystal structures that preserve crystal symmetry. In this study, we leverage novel diffusion probabilistic (DP) models to denoise atomic coordinates rather than adopting the standard score matching approach in CDVAE. Our proposed DP-CDVAE model can reconstruct and generate crystal structures whose qualities are statistically comparable to those of the original CDVAE. Furthermore, notably, when comparing the carbon structures generated by the DP-CDVAE model with relaxed structures obtained from density functional theory calculations, we find that the DP-CDVAE generated structures are remarkably closer to their respective ground states. The energy differences between these structures and the true ground states are, on average, 68.1 meV/atom lower than those generated by the original CDVAE. This significant improvement in the energy accuracy highlights the effectiveness of the DP-CDVAE model in generating crystal structures that better represent their ground-state configurations.

SUBMITTER: Pakornchote T

PROVIDER: S-EPMC10787843 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature

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Diffusion probabilistic models enhance variational autoencoder for crystal structure generative modeling.

Pakornchote Teerachote T Choomphon-Anomakhun Natthaphon N Arrerut Sorrjit S Atthapak Chayanon C Khamkaeo Sakarn S Chotibut Thiparat T Bovornratanaraks Thiti T

Scientific reports 20240113 1

The crystal diffusion variational autoencoder (CDVAE) is a machine learning model that leverages score matching to generate realistic crystal structures that preserve crystal symmetry. In this study, we leverage novel diffusion probabilistic (DP) models to denoise atomic coordinates rather than adopting the standard score matching approach in CDVAE. Our proposed DP-CDVAE model can reconstruct and generate crystal structures whose qualities are statistically comparable to those of the original CD ...[more]

PMID: 38218957

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Project description:Predicting changes in protein thermostability due to amino acid substitutions is essential for understanding human diseases and engineering useful proteins for clinical and industrial applications. While recent advances in protein generative models, which learn probability distributions over amino acids conditioned on structural or evolutionary sequence contexts, have shown impressive performance in predicting various protein properties without task-specific training, their strong unsupervised prediction ability does not extend to all protein functions. In particular, their potential to improve protein stability prediction remains underexplored. In this work, we present SPURS, a novel deep learning framework that adapts and integrates two general-purpose protein generative models-a protein language model (ESM) and an inverse folding model (ProteinMPNN)-into an effective stability predictor. SPURS employs a lightweight neural network module to rewire per-residue structure representations learned by ProteinMPNN into the attention layers of ESM, thereby informing and enhancing ESM's sequence representation learning. This rewiring strategy enables SPURS to harness evolutionary patterns from both sequence and structure data, where the sequence likelihood distribution learned by ESM is conditioned on structure priors encoded by ProteinMPNN to predict mutation effects. We steer this integrated framework to a stability prediction model through supervised training on a recently released mega-scale thermostability dataset. Evaluations across 12 benchmark datasets showed that SPURS delivers accurate, rapid, scalable, and generalizable stability predictions, consistently outperforming current state-of-the-art methods. Notably, SPURS demonstrates remarkable versatility in protein stability and function analyses: when combined with a protein language model, it accurately identifies protein functional sites in an unsupervised manner. Additionally, it enhances current low-N protein fitness prediction models by serving as a stability prior model to improve accuracy. These results highlight SPURS as a powerful tool to advance current protein stability prediction and machine learning-guided protein engineering workflows. The source code of SPURS is available at https://github.com/luo-group/SPURS.

Dataset Information

Diffusion probabilistic models enhance variational autoencoder for crystal structure generative modeling.

Publications

Diffusion probabilistic models enhance variational autoencoder for crystal structure generative modeling.

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