Folding alpha-helical membrane proteins into liposomes in vitro and determination of secondary structure

Research output: Chapter in Book/Report/Conference proceedingPoster abstract

7 Citations (Scopus)


The native environment of integral membrane proteins is a highly complex lipid bilayer composed of many different types of lipids, the physical characteristics of which can profoundly influence protein stability, folding, and function. Secondary transporters are a class of protein where changes to both structure and activity have been observed in different bilayer environments. In order to study these interactions in vitro, it is necessary to extract and purify the protein and exchange it into an artificial lipid system that can be manipulated to control protein behavior. Liposomes are a commonly used model system that is particularly suitable for studying transporters. GalP and LacY can be reconstituted or refolded into vesicles with a high degree of efficiency for further structural analysis. Circular dichroism spectroscopy is an important technique in monitoring protein folding, which allows the decomposition of spectra into secondary structural components.

Original languageEnglish
Title of host publicationMembrane Proteins
Subtitle of host publicationFolding, Association, and Design
EditorsGiovanna Ghirlanda, Alessandro Senes
PublisherHumana Press
Number of pages8
ISBN (Print)9781627035828
Publication statusE-pub ahead of print - 31 Jul 2013

Publication series

NameMethods in Molecular Biology
PublisherHumana Press
ISSN (Print)1064-3745


  • Calcium-Binding Proteins
  • Liposomes
  • Membrane Proteins
  • Monosaccharide Transport Proteins
  • Periplasmic Binding Proteins
  • Protein Denaturation
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sucrose


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