Ligandal ΔForge is the energetic ground-truth engine powering LigandAI's peptide and protein binder design platform. Using linear-time O(n) thermodynamic scoring, ΔForge computes residue-level ΔΔG contributions across protein-protein interfaces through rigorous physics-based decomposition—integrating Lennard-Jones potentials, Coulombic electrostatics, Morse-potential hydrogen bonding, hydrophobic burial energetics, and orientation-aware geometric constraints. This enables exhaustive mutational landscape exploration at speeds orders of magnitude faster than molecular dynamics, transforming weeks of traditional computation into seconds of precise energetic insight. ΔForge systematically identifies affinity-enhancing mutations (ΔΔG < 0) while preserving the structural integrity essential for experimental success.
id: scarlet-ox-pearl

Nipah Virus Glycoprotein G
0.31
80.17
--
15.1 kDa
137
id: pale-vole-quartz

Nipah Virus Glycoprotein G
0.59
35.67
--
15.5 kDa
137
id: ivory-bison-pearl

Nipah Virus Glycoprotein G
0.34
65.15
--
15.1 kDa
137
id: solid-boar-ivy

Nipah Virus Glycoprotein G
0.40
23.74
--
15.5 kDa
137
id: azure-mole-vine

Nipah Virus Glycoprotein G
0.03
58.87
--
15.2 kDa
137
id: deep-lynx-iron

Nipah Virus Glycoprotein G
0.09
55.30
--
15.2 kDa
137
id: dark-quail-pine

Nipah Virus Glycoprotein G
0.79
79.96
--
15.0 kDa
137
id: pale-seal-iron

Nipah Virus Glycoprotein G
0.02
63.31
--
15.1 kDa
137
id: calm-bee-dust

Nipah Virus Glycoprotein G
0.56
65.05
--
15.1 kDa
137
id: jade-kiwi-thorn

Nipah Virus Glycoprotein G
0.01
83.75
--
15.3 kDa
137