Thermodynamic benchmark study using Biacore technology
| العنوان: | Thermodynamic benchmark study using Biacore technology |
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| المؤلفون: | Susan Brophy, Xiaochun Qin, Rebecca L. Rich, Mary M. Murphy, Hann-Wen Guan, Nenad Tomasevic, Tanya Hayden, Giuseppe A. Papalia, Stephanie Leavitt, Brad Condon, Ta Deng, Fabio Parmeggiani, Thomas Heutmekers, Daniel Bedinger, Terry Nakagawa, Iva Navratilova, Tiffany Tsang, Bart Hoorelbeke, David G. Myszka, M. Brett Waddell, Fred Feiyu Zhang, Sabina Rebe, Mark C. McCroskey, Anne W Emerick |
| المصدر: | Analytical Biochemistry, 364(1), 67-77 Analytical Biochemistry 364 (2007) 1 |
| بيانات النشر: | Elsevier BV, 2007. |
| سنة النشر: | 2007 |
| مصطلحات موضوعية: | Biomedical Research, binding, Carbonic anhydrase II, RIKILT - Business Unit Veiligheid & Gezondheid, Biophysics, Thermodynamics, Biosensing Techniques, Calorimetry, users, Carbonic Anhydrase II, equilibrium, Biochemistry, Dissociation (chemistry), surface, Surface plasmon resonance, Carbonic Anhydrase Inhibitors, Molecular Biology, Observer Variation, Sulfonamides, Chromatography, Chemistry, Protein protein, Isothermal titration calorimetry, Cell Biology, Surface Plasmon Resonance, Benchmarking, RIKILT - Business Unit Safety & Health, Observer variation, Biosensor, Protein Binding |
| الوصف: | 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 four sulfonamide-based inhibitors) and were instructed to collect response data from 6 to 36 °C. van’t Hoff enthalpies and entropies were calculated from the temperature dependence of the binding constants. The equilibrium dissociation and thermodynamic constants determined from the Biacore analysis matched the values determined using isothermal titration calorimetry. These results demonstrate that immobilization of the enzyme onto the sensor surface did not alter the thermodynamics of these interactions. This benchmark study also provides insights into the opportunities and challenges in carrying out thermodynamic studies using optical biosensors. |
| وصف الملف: | application/octet-stream; application/pdf |
| تدمد: | 0003-2697 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::405bdba119b3472d89e841de4753f898Test https://doi.org/10.1016/j.ab.2007.01.031Test |
| حقوق: | RESTRICTED |
| رقم الانضمام: | edsair.doi.dedup.....405bdba119b3472d89e841de4753f898 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00032697 |
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