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Theoretical Modeling of Oligopeptides through Capillary Electrophoresis and Tarnsport Studies

Twahir, Umar T
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Abstract

Within this study, the focus will be on oligoglycines. Numerous studies pertaining to the mobility and conformations of oligoglycines have been completed, as this is a driving force for the study. The oligopeptide is modeled using a “coarse-grained” model created in the Allison lab at Georgia State University [Xin,Y.,et. al, J. Phys. Chem. B 2006, 110, 1038-1045], which will be briefly explained within this paper. Oligoglycines will be studied in a few different systems, as the overall charge on the peptide and system will affect its mobility. The conclusion drawn is that the peptide adopts three different conformations based on the temperature of the system and length of the peptide; random conformation at high temperatures, and compact conformations at low temperature. Oligoglycines of length three to five amino acids adopts a cyclic conformation at low temperatures. [Allison, S., et al., J. Sep. Sci. 2010, 33, 2430- 2438.]

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2011-04-04
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Electrophoretic effect, Relaxation effect, Complex formation, Electrophoretic mobility, Electrophoretic mobility of peptides
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