@article {1107,
title = {Enumeration algorithm for determination of binding constants in capillary electrophoresis},
journal = {Analytical Chemistry},
volume = {77},
number = {8},
year = {2005},
note = {ISI Document Delivery No.: 919FZTimes Cited: 11Cited Reference Count: 16},
month = {Apr},
pages = {2415-2420},
type = {Article},
abstract = {With more accurate simulation models and more efficient algorithms becoming available, the binding constants of an affinity interaction can be obtained from much simpler experiments using capillary electrophoresis. With the enumeration algorithm, all possible combinations of the binding constant and the complex mobility in certain ranges that could result in the experimental migration time of an injected analyte are extracted from a 3-D surface, which depicts the migration times resulting from different values of the binding constant and the mobility of the complex formed between the interacting pair, to form a 2-D curve. When the experimental conditions are changed, the analyte migration time will also change. A new 2-D curve can be constructed from another 3-D surface on the basis of the pairs of binding constants and complex mobility values that could result in the new migration time. Because the true binding constant and complex mobility values have to be the same for both experimental conditions under the same temperature, there has to be a point where both 2-D curves will converge. The coordinates of the converging point give the values for a binding constant and a complex mobility that will fit all 2-D curves generated under certain experimental conditions. p-Nitrophenol is used as the analyte, beta-cyclodextrin is used as the additive, and a one-cell model is used to simulate affinity CE. The experimental conditions that can improve the accuracy of the binding constants are discussed.},
keywords = {DYNAMIC COMPLEXATION, ERROR PROPAGATION, MIGRATION BEHAVIOR, MONTE-CARLO-SIMULATION, NUMERICAL-SIMULATION, QUANTITATIVE DESCRIPTION, RANGE, RECTANGULAR HYPERBOLAE, SEPARATION, ZONE-ELECTROPHORESIS},
isbn = {0003-2700},
url = {://000228605100018},
author = {Fang, N. and Chen, D. D. Y.}
}
@article {1108,
title = {General approach to high-efficiency simulation of affinity capillary electrophoresis},
journal = {Analytical Chemistry},
volume = {77},
number = {3},
year = {2005},
note = {ISI Document Delivery No.: 893ZGTimes Cited: 12Cited Reference Count: 22},
month = {Feb},
pages = {840-847},
type = {Article},
abstract = {The differential equation describing electrophoretic migration can be evaluated with various finite difference schemes (FDSs). However, the accuracy and efficiency can be dramatically different depending on the FDS chosen and the way the algorithm is implemented in a computer simulation program. The monotonic transport scheme is used as the algorithm for the hyperbolic part of the differential equation, and the first-order fully explicit scheme is used for the parabolic part of the equation. The combination of these algorithms minimizes the errors and maintains high efficiency. A circular arrangement of the cells in the computer{\textquoteright}s memory is used in the implementation of the algorithms, and the use of concentration thresholds to enable and disable cells along the capillary makes the new algorithm highly efficient. Either thermodynamic or kinetic constants can be used in this program to simulate binding interactions between two species for equilibrium and nonequilibrium affinity CE. Simulation results with various parameters are presented. The simulated peak with proper parameters for an equilibrium affinity CE experiment has shape and position similar to that of the experimental peak. The simulated electropherograms for a nonequilibrium affinity CE experiment also show characteristics of the experimental electropherograms.},
keywords = {COMPUTER-SIMULATION, ELECTROMIGRATION, EQUILIBRIUM MIXTURES, MATHEMATICAL-MODEL, NUMERICAL-SIMULATION, SEPARATIONS, ZONE-ELECTROPHORESIS},
isbn = {0003-2700},
url = {://000226759000024},
author = {Fang, N. and Chen, D. D. Y.}
}
@article {849,
title = {Determination of shapes and maximums of analyte peaks based on solute mobilitiess in capillary electrophoresis},
journal = {Analytical Chemistry},
volume = {76},
number = {6},
year = {2004},
note = {ISI Document Delivery No.: 803IQTimes Cited: 11Cited Reference Count: 28},
month = {Mar},
pages = {1708-1714},
type = {Article},
abstract = {In capillary electrophoresis, the relative orders of mobilities of analyte, additive, and the complex formed determine the analyte peak shape in a way similar to the way the binding isotherms determine the peak shapes in chromatography. The three mobilities allow six possible orders; each produces a characteristic peak shape in CE. Equations describing the analyte migration in a CE system with the presence of mobility-changing additives can be implemented into computer programs to predict the migration times of the analyte peak maximums, and the predicted migration times agree well with the experimental results.},
keywords = {DISPERSION, DYNAMIC COMPLEXATION, FLOW, MIGRATION BEHAVIOR, NUMERICAL-SIMULATION, pressure, QUANTITATIVE DESCRIPTION, SEPARATIONS, ZONE-ELECTROPHORESIS},
isbn = {0003-2700},
url = {://000220225200023},
author = {Fang, N. and Ting, E. and Chen, D. D. Y.}
}