ConfRover: Simultaneous Modeling of Protein Conformation and Dynamics via Autoregression

Fuente: arXiv
Saved in:
Bibliographic Details
Main Authors: Shen, Yuning, Wang, Lihao, Yuan, Huizhuo, Wang, Yan, Yang, Bangji, Gu, Quanquan
Format: Preprint
Published: 2025
Subjects:
Online Access:
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1866914178030108672
author Shen, Yuning
Wang, Lihao
Yuan, Huizhuo
Wang, Yan
Yang, Bangji
Gu, Quanquan
author_facet Shen, Yuning
Wang, Lihao
Yuan, Huizhuo
Wang, Yan
Yang, Bangji
Gu, Quanquan
contents Understanding protein dynamics is critical for elucidating their biological functions. The increasing availability of molecular dynamics (MD) data enables the training of deep generative models to efficiently explore the conformational space of proteins. However, existing approaches either fail to explicitly capture the temporal dependencies between conformations or do not support direct generation of time-independent samples. To address these limitations, we introduce ConfRover, an autoregressive model that simultaneously learns protein conformation and dynamics from MD trajectories, supporting both time-dependent and time-independent sampling. At the core of our model is a modular architecture comprising: (i) an encoding layer, adapted from protein folding models, that embeds protein-specific information and conformation at each time frame into a latent space; (ii) a temporal module, a sequence model that captures conformational dynamics across frames; and (iii) an SE(3) diffusion model as the structure decoder, generating conformations in continuous space. Experiments on ATLAS, a large-scale protein MD dataset of diverse structures, demonstrate the effectiveness of our model in learning conformational dynamics and supporting a wide range of downstream tasks. ConfRover is the first model to sample both protein conformations and trajectories within a single framework, offering a novel and flexible approach for learning from protein MD data. Project website: https://bytedance-seed.github.io/ConfRover.
format Preprint
id arxiv_https___arxiv_org_abs_2505_17478
institution arXiv
publishDate 2025
record_format arxiv
spellingShingle ConfRover: Simultaneous Modeling of Protein Conformation and Dynamics via Autoregression
Shen, Yuning
Wang, Lihao
Yuan, Huizhuo
Wang, Yan
Yang, Bangji
Gu, Quanquan
Machine Learning
Artificial Intelligence
Biological Physics
Biomolecules
Quantitative Methods
Understanding protein dynamics is critical for elucidating their biological functions. The increasing availability of molecular dynamics (MD) data enables the training of deep generative models to efficiently explore the conformational space of proteins. However, existing approaches either fail to explicitly capture the temporal dependencies between conformations or do not support direct generation of time-independent samples. To address these limitations, we introduce ConfRover, an autoregressive model that simultaneously learns protein conformation and dynamics from MD trajectories, supporting both time-dependent and time-independent sampling. At the core of our model is a modular architecture comprising: (i) an encoding layer, adapted from protein folding models, that embeds protein-specific information and conformation at each time frame into a latent space; (ii) a temporal module, a sequence model that captures conformational dynamics across frames; and (iii) an SE(3) diffusion model as the structure decoder, generating conformations in continuous space. Experiments on ATLAS, a large-scale protein MD dataset of diverse structures, demonstrate the effectiveness of our model in learning conformational dynamics and supporting a wide range of downstream tasks. ConfRover is the first model to sample both protein conformations and trajectories within a single framework, offering a novel and flexible approach for learning from protein MD data. Project website: https://bytedance-seed.github.io/ConfRover.
title ConfRover: Simultaneous Modeling of Protein Conformation and Dynamics via Autoregression
topic Machine Learning
Artificial Intelligence
Biological Physics
Biomolecules
Quantitative Methods
url https://arxiv.org/abs/2505.17478