The Role of Protein Structure in Chromatographic Behavior
- 16 October 1987
- journal article
- review article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 238 (4825), 319-323
- https://doi.org/10.1126/science.3310233
Abstract
Chromatographic retention is determined by a relatively small number of amino acids located in a chromatographic contact region on the surface of a polypeptide. This region is determined by the mode of separation and the amino acid distribution within the polypeptide. The contact area may be as small as a few hundred square angstroms in bioaffinity chromatography. In contrast, the contact region in ion exchange, reversed phase, hydrophobic interaction and the other nonbioaffinity separation modes is much broader, ranging from one side to the whole external surface of a polypeptide. Furthermore, structural changes that alter the chromatographic contact region will alter chromatographic properties. Thus, although immunosorbents can be very useful in purifying proteins of similar primary structure, they will be ineffective in discriminating between small, random variations within a structure. Nonbioaffinity columns complement affinity columns in probing a much larger portion of solute surface and being able to discriminate between protein variants.Keywords
This publication has 26 references indexed in Scilit:
- Retention mechanism of lactate dehydrogenase in anion-exchange chromatographyJournal of Chromatography A, 1987
- Application of the stoichiometric displacement model of retention to anion-exchange chromatography of nucleic acidsJournal of Chromatography A, 1986
- Solute and mobile phase contributions to retention in hydrophobic interaction chromatography of proteinsJournal of Chromatography A, 1986
- Effects of high-performance liquid chromatographic solvents and hydrophobic matrices on the secondary and quarternary structure of a model protein : Reversed-phase and size-exclusion high-performance liquid chromatographyJournal of Chromatography A, 1984
- Protein conformation and reversed-phase high-performance liquid chromatographyJournal of Chromatography A, 1984
- Salt-mediated retention of proteins in hydrophobic-interaction chromatography : Application of solvophobic theoryJournal of Chromatography A, 1984
- Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt bindingBiochemistry, 1984
- Multiple peak formation in reversed-phase liquid chromatography of papainAnalytical Chemistry, 1984
- Evaluation of a retention model for high-performance ion-exchange chromatography using two different displacing saltsJournal of Chromatography A, 1984
- Crystal structure of Turkey egg-white lysozyme: Results of the molecular replacement method at 5 Å resolutionJournal of Molecular Biology, 1976