arXiv:2606. 14737v1 Announce Type: cross Abstract: Molecular dynamics (MD) simulations generate trajectories in a high-dimensional configuration space whose analysis critically depends on molecular descriptors, typically handcrafted observables or learned kinetic embeddings.
arXiv:2410.20317v2 Announce Type: replace Abstract: Molecular dynamics (MD) simulations are a principled but computationally expensive approach for studying protein conformational variability, making...
arXiv:2607. 15309v1 Announce Type: cross Abstract: Proteins function through coordinated motion across multiple spatial and temporal scales, underpinning processes such as ligand binding, allostery, and catalysis.
arXiv:2605. 01625v3 Announce Type: replace Abstract: Proteins are inherently multiscale physical systems whose functional properties emerge from coordinated structural organization across multiple spatial resolutions, ranging from atomic interactions to global fold topology.
arXiv:2512. 18454v3 Announce Type: replace Abstract: Predictive machine learning models generally excel on in-distribution data, but their performance degrades on out-of-distribution (OOD) inputs.
arXiv:2608. 09099v1 Announce Type: new Abstract: Quantitative estimation of protein-ligand binding affinity from three-dimensional complex structures is a fundamental task in structure-based computational chemistry and molecular modeling.
arXiv:2606. 08375v1 Announce Type: new Abstract: All-atom generative modeling of 3D biomolecular complexes has emerged as the dominant paradigm for predicting the structure of proteins and protein-ligand systems.
arXiv:2603. 19636v2 Announce Type: replace Abstract: Accurate RNA structure modeling remains difficult because RNA backbones are highly flexible, non-canonical interactions are prevalent, and experimentally determined 3D structures are comparatively scarce.
arXiv:2610.02186v1 Announce Type: cross Abstract: Molecular learning models are strongly shaped by their underlying representations. Yet standard sequential and graph formalisms struggle to explicitl...
arXiv:2512. 15133v3 Announce Type: replace-cross Abstract: Proteins inherently possess a consistent sequence-structure duality.
arXiv:2504. 02839v2 Announce Type: replace-cross Abstract: Proteins move and deform to ensure their biological functions.
arXiv:2608.29207v1 Announce Type: new Abstract: Protein structure modeling rests on a single computational primitive: the interaction between what a residue is (sequence content) and where it sits (t...
arXiv:2605. 02937v2 Announce Type: replace-cross Abstract: Deep learning in de novo protein design has achieved atomic-level fidelity.