arXiv:2606. 23830v1 Announce Type: cross Abstract: Molecular surfaces encode the geometric and physicochemical patterns that determine antibody-antigen recognition, central to epitope prediction.
Summary generated by The Flow from the publisher's feed. The full article lives at arXiv AI.
arXiv:2606. 07567v1 Announce Type: cross Abstract: Protein function is largely determined by molecular surface geometry and physicochemical complementarity, yet most protein design methods condition only on backbone structure.
arXiv:2606. 04154v1 Announce Type: cross Abstract: Antibodies neutralize foreign antigens by binding to specific surface regions called epitopes.
arXiv:2605. 21600v2 Announce Type: replace Abstract: Computational antibody CDR design methods condition on antigen structure to generate binding loops.
arXiv:2606. 14217v1 Announce Type: new Abstract: Accurate prediction of protein-ligand binding affinity is essential for structure-based drug discovery.
arXiv:2606. 14159v1 Announce Type: new Abstract: Protein-ligand binding affinity (PLA) prediction is critical in drug discovery.
arXiv:2606. 28659v1 Announce Type: cross Abstract: High-fidelity molecular docking simulations can produce biologically relevant estimates of epitope-receptor binding affinity but are computationally expensive and therefore limit the number of candidates that can be screened for vaccine design.