Protein conformation and reversed-phase high-performance liquid chromatography

The structure of a series of proteins has been investigated by circular dichroism, fluorescence and visible spectroscopy as well as by differential scanning calorimetry under reversed-phase high-performance liquid chromatography elution conditions. These studies show that 1-propanol, a typical eluen...

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Bibliographic Details
Published in:	Journal of chromatography Vol. 317; p. 93
Main Authors:	Sadler, A J, Micanovic, R, Katzenstein, G E, Lewis, R V, Middaugh, C R
Format:	Journal Article
Language:	English
Published:	Netherlands 01-01-1984
Subjects:	1-Propanol Calorimetry, Differential Scanning Chemical Phenomena Chemistry, Physical Chromatography, High Pressure Liquid Circular Dichroism Humans Hydrogen-Ion Concentration Protein Conformation Solvents Spectrometry, Fluorescence
Online Access:	Get more information
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Summary:	The structure of a series of proteins has been investigated by circular dichroism, fluorescence and visible spectroscopy as well as by differential scanning calorimetry under reversed-phase high-performance liquid chromatography elution conditions. These studies show that 1-propanol, a typical eluent, induces a reversible conformational change in proteins to an apparently ordered, helical form. This structural transition occurs in the range of propanol concentrations that produces elution of a particular protein. The possible relationship between this conformational change and protein elution is considered.
DOI:	10.1016/S0021-9673(01)91650-4