Thermodynamic benchmark study using Biacore technology

• Published in: Analytical biochemistry Vol. 364; no. 1; pp. 67 - 77
• Main Authors: Navratilova, Iva, Papalia, Giuseppe A., Rich, Rebecca L., Bedinger, Daniel, Brophy, Susan, Condon, Brad, Deng, Ta, Emerick, Anne W., Guan, Hann-Wen, Hayden, Tanya, Heutmekers, Thomas, Hoorelbeke, Bart, McCroskey, Mark C., Murphy, Mary M., Nakagawa, Terry, Parmeggiani, Fabio, Qin, Xiaochun, Rebe, Sabina, Tomasevic, Nenad, Tsang, Tiffany, Waddell, M. Brett, Zhang, Fred Feiyu, Leavitt, Stephanie, Myszka, David G.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.05.2007
• Subjects: Affinity; Benchmarking; binding; Biomedical Research; Biosensing Techniques - instrumentation; Biosensing Techniques - standards; Biosensor; Calorimetry - instrumentation; Calorimetry - standards; Carbonic Anhydrase II - chemistry; Carbonic Anhydrase II - metabolism; Carbonic Anhydrase Inhibitors - classification; Carbonic Anhydrase Inhibitors - metabolism; equilibrium; Kinetics; Observer Variation; Protein Binding; Protein–protein; SPR; Sulfonamides - antagonists & inhibitors; Sulfonamides - classification; surface; Surface Plasmon Resonance - instrumentation; Surface Plasmon Resonance - standards; Thermodynamics; users; Affinity; Kinetics; SPR; Biosensor; Protein–protein

A total of 22 individuals participated in this benchmark study to characterize the thermodynamics of small-molecule inhibitor–enzyme interactions using Biacore instruments. Participants were provided with reagents (the enzyme carbonic anhydrase II, which was immobilized onto the sensor surface, and...