Conformational effects in reversed-phase high-performance liquid chromatography of polypeptides I. Resolution of insulin variants
- 8 September 1995
- journal article
- Published by Elsevier BV in Journal of Chromatography A
- Vol. 711 (1), 61-70
- https://doi.org/10.1016/0021-9673(95)00241-e
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- High-performance liquid chromatography of amino acids, peptides, and proteins. 123. Dynamics of peptides in reversed-phase high-performance liquid chromatographyAnalytical Chemistry, 1993
- Acid stabilization of insulinBiochemistry, 1993
- The A14 position of insulin tolerates considerable structural alterations with modest effects on the biological behavior of the hormoneJournal of Protein Chemistry, 1992
- Structure and evolution of insulins: Implications for receptor bindingBioEssays, 1992
- Receptor binding redefined by a structural switch in a mutant human insulinNature, 1991
- Toward the solution structure of human insulin: sequential 2D proton NMR assignment of a des-pentapeptide analog and comparison with crystal structureBiochemistry, 1990
- Complete sequence-specific proton NMR assignments for human insulinBiochemistry, 1990
- Solute and mobile phase contributions to retention in hydrophobic interaction chromatography of proteinsJournal of Chromatography A, 1986
- Three mutant insulins in manNature, 1983
- Stability of bovine insulinJournal of Pharmacy and Pharmacology, 1981