@article {1389,
	title = {Behavior of interacting species in capillary electrophoresis described by mass transfer equation},
	journal = {Analytical Chemistry},
	volume = {78},
	number = {6},
	year = {2006},
	note = {ISI Document Delivery No.: 025ZYTimes Cited: 9Cited Reference Count: 30},
	month = {Mar},
	pages = {1832-1840},
	type = {Article},
	abstract = {Affinity capillary electrophoresis (ACE) has been used to estimate thermodynamic constants of binding interactions with linear or nonlinear regression methods. The accuracy of this approach relies heavily on the binding interaction mechanism, which is controlled by both the nature of the interaction and the experimental conditions. The development of a highly efficient computer-simulated ACE system makes it possible to demonstrate the detailed behavior of any interacting species of a given interaction under any conditions. The order of the mobilities of the complex and the two binding species in their free forms is a key factor to determine what molecules in what locations of the column are involved in the interaction, and the peak shape resulting from such interactions, of a given ACE experiment. In this paper and the supporting materials, 18 scenarios in 6 different combinations of migration orders of the free analyte, free additive, and complex formed are studied by a computer simulation program based on the mass transfer equation. From the study of these situations, we conclude high additive concentration (ensuring high capacity factor) and low analyte concentration (ensuring fast fill-in of the free additive in the analyte plug) are crucial for obtaining accurate results when using the regression methods. On the other hand, the approach to estimate binding constants with computer simulation can be much more accurate as long as accurate and efficient simulation models can be developed, especially when the ratio of the additive and analyte concentrations is not large enough.},
	keywords = {BINDING CONSTANTS, CHROMATOGRAPHY, DISPERSION, EFFICIENCY, ERROR PROPAGATION, MONTE-CARLO-SIMULATION, pressure, RECTANGULAR HYPERBOLAE, SEPARATIONS, ZONE-ELECTROPHORESIS},
	isbn = {0003-2700},
	url = {<Go to ISI>://000236307700015},
	author = {Fang, N. and Chen, D. D. Y.}
}
@article {1356,
	title = {Collision-induced alignment of H2O+ drifting in helium},
	journal = {Journal of Chemical Physics},
	volume = {124},
	number = {17},
	year = {2006},
	note = {ISI Document Delivery No.: 039QQTimes Cited: 0Cited Reference Count: 27},
	month = {May},
	pages = {8},
	type = {Article},
	abstract = {The collision-induced alignment of H2O+ drifting in helium is studied with a molecular dynamics method that has been extended to treat nonlinear rigid ions. Rotational distribution functions and averaged quantities are presented in terms of the rho formalism [M. Thachuk, Phys. Rev. A 72, 032722 (2005)], and it is shown that this description gives a very good agreement with simulation results. In addition to velocity and angular velocity autocorrelation functions, a velocity-angular velocity cross correlation function is introduced. This cross correlation function provides insight into the dynamical nature of the alignment mechanism. 2006 American Institute of Physics.},
	keywords = {CROSS-SECTIONS, CYTOCHROME-C, ELECTROSTATIC FIELDS, IN-VACUO, INTRINSIC SIZE PARAMETERS, ION-MOTION, MOLECULAR-DYNAMICS, MONTE-CARLO-SIMULATION, POTENTIAL-ENERGY SURFACES, ROTATIONAL ALIGNMENT},
	isbn = {0021-9606},
	url = {<Go to ISI>://000237321700019},
	author = {Chen, X. and Thachuk, M.}
}
@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 = {<Go to ISI>://000228605100018},
	author = {Fang, N. and Chen, D. D. Y.}
}
