@article {1225,
	title = {Entropic interaction chromatography: Separating proteins on the basis of size using end-grafted polymer brushes},
	journal = {Biotechnology and Bioengineering},
	volume = {90},
	number = {1},
	year = {2005},
	note = {ISI Document Delivery No.: 909ETTimes Cited: 9Cited Reference Count: 48},
	month = {Apr},
	pages = {1-13},
	type = {Article},
	abstract = {Partitioning of a macromolecule into the interfacial volume occupied by a grafted polymer brush decreases the configurational entropy (Delta S(c)brush) of the terminally attached linear polymer chains due to a loss of free volume. Self-consistent field theory (SCF) calculations are used to show that Delta S(c)brush is a strong function of both the size (MW,) of the partitioning macromolecule and the depth of penetration into the brush volume. We further demonstrate that the strong dependence of Delta S(c)brush on MW, provides a novel and powerful platform, which we call entropic interaction chromatography (EIC), for efficiently separating mixtures of proteins on the basis of size. Two EIC columns, differing primarily in polymer grafting density, were prepared by growing a brush of poly(methoxyethyl acrylamide) chains on the surface of a widepore (1,000-angstrom pores, 64-mu m diameter rigid beads) resin (Toyopearl AF-650M) bearing surface aldehyde groups. Semipreparative 0.1-L columns packed with either EIC resin provide reduced-plate heights of 2 or less for efficient separation of globular protein mixtures over at least three molecular-weight decades. Protein partitioning within these wide-pore EIC columns is shown to be effectively modeled as a thermodynamically controlled process, allowing partition coefficients (K-p) and elution chromatograms to be accurately predicted using a column model that combines SCF calculation of Kp values with an equilibrium-dispersion type model of solute transport through the column. This model is used to explore the dependence of column separation efficiency on brush properties, predicting that optimal separation of proteins over a broad MW, range is achieved at low to moderate grafting densities and intermediate chain lengths. (c) 2005 Wiley Periodicals, Inc.},
	keywords = {ADSORPTION, CHAIN MOLECULES, CONSISTENT-FIELD THEORY, entropic interaction chromatography, equilibrium dispersion, EXCLUSION CHROMATOGRAPHY, GEL FILTRATION, grafted polymer brush, HUMAN SERUM-ALBUMIN, LIQUID-CHROMATOGRAPHY, MODEL, MOLECULAR-WEIGHT, MONTE-CARLO, protein purification, size exclusion chromatography, STATISTICAL-THEORY},
	isbn = {0006-3592},
	url = {<Go to ISI>://000227843800001},
	author = {Pang, P. and Koska, J. and Coad, B. R. and Brooks, D. E. and Haynes, C. A.}
}
@article {3518,
	title = {A CONFIGURATION BIAS MONTE-CARLO METHOD FOR WATER},
	journal = {Journal of Chemical Physics},
	volume = {102},
	number = {19},
	year = {1995},
	note = {ISI Document Delivery No.: QX773Times Cited: 29Cited Reference Count: 24},
	month = {May},
	pages = {7656-7663},
	type = {Article},
	keywords = {CANONICAL ENSEMBLE, CHAIN MOLECULES, CHEMICAL-POTENTIALS, DYNAMICS, SIMULATION},
	isbn = {0021-9606},
	url = {<Go to ISI>://A1995QX77300041},
	author = {Shelley, J. C. and Patey, G. N.}
}
@article {3162,
	title = {A CONFIGURATION BIAS MONTE-CARLO METHOD FOR IONIC-SOLUTIONS},
	journal = {Journal of Chemical Physics},
	volume = {100},
	number = {11},
	year = {1994},
	note = {ISI Document Delivery No.: NN731Times Cited: 5Cited Reference Count: 24},
	month = {Jun},
	pages = {8265-8270},
	type = {Article},
	abstract = {A version of configuration bias Monte Carlo suitable for the insertion and deletion of ions in grand canonical Monte Carlo simulations of ionic solutions has been developed. The method has been optimized and applied to a system where the straightforward insertion and deletion of ions is prohibitively impractical. The present approach is likely to be useful in other systems as well.},
	keywords = {CHAIN MOLECULES, DIPOLAR LIQUIDS},
	isbn = {0021-9606},
	url = {<Go to ISI>://A1994NN73100044},
	author = {Shelley, J. C. and Patey, G. N.}
}
