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CIR-DDG: backbone-agnostic residual correction of antibody-antigen affinity changes with explicit cross-chain geometry

Yu, Weilun et al.
arXiv (OAI Expanded) · Papers
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quantitative-methods
Motivation: Accurate prediction of mutation-induced protein--protein binding free-energy changes is important for antibody affinity maturation, yet scarce labels and complex interface geometry limit generalization. Heterogeneous predictors may process three-dimensional complexes without preserving t
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