Comparison of ultrafiltration units for proteomic and N-glycoproteomic analysis by the filter-aided sample preparation method |
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Authors: | Wiśniewski Jacek R Zielinska Dorota F Mann Matthias |
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Affiliation: | Molecular Biophysics, University of Kaiserslautern, 67663 Kaiserslautern, Germany |
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Abstract: | The precision with which the dissociation constant, KD, can be obtained from isothermal titration calorimetry depends on, among other factors, the concentrations of the interacting species. The so-called c value—the ratio of analyte concentration to KD—should fall in the range of 1 to 1000 for reliable KD determination. On the basis of simulated, noise-free data, Biswas and Tsodikov [5] recently suggested an optimal c value of 5 to 20. By contrast, we find an optimum at c > 40 on determining the KD confidence intervals through simulations containing noise levels typical of state-of-the-art microcalorimeters. |
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Keywords: | Dissociation constant KD window Precision Simulation Error analysis |
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