Jump to main content
Jump to site search

Issue 20, 2016
Previous Article Next Article

On-line determination by small angle X-ray scattering of the shape of hen egg white lysozyme immediately following elution from a hydrophobic interaction chromatography column

Author affiliations

Abstract

This study documents the use of an integrated approach, involving on-line hydrophobic interaction chromatography interfaced with Small Angle X-ray Scattering (HIC–SAXS) measurements, to monitor the conformational status of proteins immediately upon elution from a chromatographic column operated at different temperatures. Moreover, this approach provides an additional avenue to interrogate the changes in protein shape that may occur across the eluted chromatographic peak. To this end, radii of gyration were extrapolated from the Guinier approximation with the HIC–SAXS data, whilst pair distribution functions and bead model simulations were generated by using the indirect transform program GNOM and ab initio reconstruction with GASBOR to provide further insight into protein conformational changes that occur during hydrophobic interaction chromatography.

Graphical abstract: On-line determination by small angle X-ray scattering of the shape of hen egg white lysozyme immediately following elution from a hydrophobic interaction chromatography column

Back to tab navigation

Publication details

The article was received on 12 Apr 2016, accepted on 02 Aug 2016 and first published on 08 Aug 2016


Article type: Paper
DOI: 10.1039/C6AN00851H
Citation: Analyst, 2016,141, 5810-5814
  •   Request permissions

    On-line determination by small angle X-ray scattering of the shape of hen egg white lysozyme immediately following elution from a hydrophobic interaction chromatography column

    C. Kulsing, A. Z. Komaromy, R. I. Boysen and M. T. W. Hearn, Analyst, 2016, 141, 5810
    DOI: 10.1039/C6AN00851H

Search articles by author

Spotlight

Advertisements