In the benchmark studies several different Biacore users are asked to measure a high affine antibody-antigen interaction, characterize the thermodynamics of small-molecule inhibitor-enzyme interaction and characterize the kinetics and affinities of 10 sulfonamide inhibitors. One large study to compare different machines and users involved 150 participants from 20 countries and used nine different instrument types.

References

(1)Katsamba, P. S. et al. Kinetic analysis of a high-affinity antibody/antigen interaction performed by multiple Biacore users. Analytical Biochemistry 352: 208-221; (2006).
(2)Navratilova, I. et al. Thermodynamic benchmark study using Biacore technology. Analytical Biochemistry 364: 67-77; (2007). Goto reference
(3)Papalia, G. A. et al. Comparative analysis of 10 small molecules binding to carbonic anhydrase II by different investigators using Biacore technology. Analytical Biochemistry 359: 94-105; (2006). Goto reference
(4)Rich, R. L. et al. A global benchmark study using affinity-based biosensors. Analytical Biochemistry (2008). Goto reference
(5)Yamniuk, A. P., S. C. Edavettal, S. Bergqvist, et al. ABRF-MIRG benchmark study: molecular interactions in a three-component system. J Biomol Tech 23: 101-14; (2012). Goto reference
(6)Myszka, D. G., Y. N. Abdiche, F. Arisaka, et al. The ABRF-MIRG'02 study: assembly state, thermodynamic, and kinetic analysis of an enzyme/inhibitor interaction. J.Biomol.Tech. 14: 247-269; (2003). Goto reference
A study where analytical ultracentrifuge, isothermal titration calorimetry and surface plasmon resonance are used to investigate the interaction between bovine carbonic anhydrase and the enzyme inhibitor 4-carboxybensenesulfonamide in terms of the assembly state, thermodynamics,affinity and kinetics of complex formation.
(7)Yamniuk, A. P., J. A. Newitt, M. L. Doyle, et al. Development of a Model Protein Interaction Pair as a Benchmarking Tool for the Quantitative Analysis of 2-Site Protein-Protein Interactions. Journal of Biomolecular Techniques : JBT 26: 125-141; (2015). Goto reference
This benchmark shows the development and characterization of a model system where one molecule has two binding sites with different affinities. Several experimental set-ups are explored to investigate the type of complex formation.