Thermodynamic Mapping of Antigen-Antibody Interfaces

To probe the relative contribution to binding of HEL residues in contact with D1.3 in the crystal structure of the FvD1.3-HEL complex. 

12 nonglycine HEL residues were individually mutated to alanine and their affinities for wild-type D1.3 measured (Dall Acqua et al., 1998). Significant decreases in binding (AAG 1 kcal/mol) were observed for 

Dissection of Binding Energetics in Antigen-Antibody Interfaces Using Double-Mutant Cycles 

In the case of the FvD1.3-FvE5.2 complex, FvDl.3 residue A and FvE5.2 residue B were mutated (i.e., A A, B B ) separately and together to construct the cycle  

Coupling Energies between Amino Acid Pairs as Measured by Double-Mutant Cycles 

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