Mouse Anti-LYZ Recombinant Antibody (clone D44.1)

Figure 1 Experimental binding affinities

From left to right: 140-fold hex, 100-fold quad, L92 Asn-to-Ala, H58 Thr-to-Asp, H57 Ser-to-Val, H28 Thr-to-Asp, wild type. For each variant, different symbol shapes distinguish independent measurements.

Lippow, S. M., Wittrup, K. D., & Tidor, B. (2007). Computational design of antibody-affinity improvement beyond in vivo maturation. Nature biotechnology, 25(10), 1171.

Figure 2 Comparison of the binding equilibrium constants at 24.0°C with literature values.

Values for K_b were determined from titration calorimetry measurements and the error is the estimated uncertainty in K_b

Schwarz, F. P., Tello, D., Goldbaum, F. A., Mariuzza, R. A., & Poljak, R. J. (1995). Thermodynamics of antigen‐antibody binding using specific anti‐lysozyme antibodies. European journal of biochemistry, 228(2), 388-394.