Abstract
A discussion of protein separation should be prefaced with a review of our general knowledge of protein structure. Proteins are biopolymers composed of an ordered sequence of acidic, basic, neutral, and hydrophobic amino acids coupled via peptide bonds. The bending and folding of this primary chain results in a secondary structure that is maintained primarily by internal hydrogen bonding. Further stabilization of the protein occurs by hydrogen, ionic, hydrophobic, covalent, and van der Waals linkages between amino acid side chains. The net result of these secondary and tertiary modifications along the polypeptide chain is a three-dimensional matrix with some amino acids buried in the interior of the protein and others exposed at the surface. As a result, proteins have specific shapes and sizes; in addition, they have areas that may be anionic, cationic, and/or hydrophobic depending on the amino acid sequence. These differences in properties make possible the chromatographic resolution of proteins.
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© 1977 Plenum Press, New York
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Regnier, F.E., Gooding, K.M., Chang, SH. (1977). High-Speed Liquid Chromatography of Proteins. In: Hercules, D.M., Hieftje, G.M., Snyder, L.R., Evenson, M.A. (eds) Contemporary Topics in Analytical and Clinical Chemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-6728-8_1
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