Modeling the electrophoresis of oligoglycines.
作者： Stuart A Allison , Hongxia Pei , Umar Twahir , Hengfu Wu , Herve Cottet
关键词: Peptide Conformation 、 Protein structure 、 Oligomer 、 Stereochemistry 、 Electrophoresis 、 Crystallography 、 Aqueous solution 、 Protein secondary structure 、 Chemistry 、 Peptide 、 Ion
摘要: The electrophoretic mobility of low molecular mass oligoglycines is examined in this study using a "coarse-grained" bead modeling methodology [Pei, H., Allison, S. A., J. Chromatogr. A 2009, 1216, 1908-1916]. advantage focusing on these peptides that their charge state well known [Plasson, R., Cottet, Anal. Chem. 2006, 78, 5394-5402] and extensive data are also available different buffers [Survay, M. Goodall, D. M., Wren, A. C., Rowe, R. 1996, 741, 99-113] over broad range temperatures Anal 2005, 77, 6047-6054]. Except for assumptions about peptide secondary structure, the B model has no adjustable parameters. It concluded adopt random configuration at high temperature (50 degrees C higher), but more compact conformations lower temperature. proposed triglycine through pentaglycine cyclic structures (up to 25 C) aqueous solution. At C, buffer interactions may or not influence conformation depending species. In borate pH, consistent with complex formation between oligoglycine anion.
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