Computationally modeling changes in binding free energies upon mutation (interface ΔΔ G)
allows large-scale prediction and perturbation of protein–protein interactions. Additionally …

Predicting the structure and thermodynamics of protein–protein interactions (PPIs) are key to
a proper understanding and modulation of their function. Since experimental methods might …

The design of proteins with novel ligand-binding functions holds great potential for
application in biomedicine and biotechnology. However, our ability to engineer ligand …

Modeling the impact of amino acid mutations on protein-protein interaction plays a crucial
role in protein engineering and drug design. In this study, we develop GeoPPI, a novel …

Understanding how gene-level mutations affect the binding affinity of protein–protein
interactions is a key issue of protein engineering. Due to the complexity of the problem …

Quantitative evaluation of binding affinity changes upon mutations is crucial for protein
engineering and drug design. Machine learning‐based methods are gaining increasing …

Motivation Most proteins perform their biological functions through interactions with other
proteins in cells. Amino acid mutations, especially those occurring at protein interfaces, can …

Interactions between small molecules and proteins play critical roles in regulating and
facilitating diverse biological functions, yet our ability to accurately re-engineer the specificity …

Purpose Mutation-induced variation of protein-ligand binding affinity is the key to many
genetic diseases and the emergence of drug resistance, and therefore predicting such …

The functional impact of protein mutations is reflected on the alteration of conformation and
thermodynamics of protein–protein interactions (PPIs). Quantifying the changes of two …