Nanodiscs as a new tool to examine lipid-protein interactions

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Nanodiscs are self-assembled discoidal fragments of lipid bilayers 8-16 nm in diameter, stabilized in solution by two amphipathic helical scaffold proteins. As stable and highly soluble membrane mimetics with controlled lipid composition and ability to add affinity tags to the scaffold protein, nanodiscs represent an attractive model system for solubilization, isolation, purification, and biophysical and biochemical studies of membrane proteins. In this chapter we overview various approaches to structural and functional studies of different classes of integral membrane proteins such as ion channels, transporters, GPCR and other receptors, membrane enzymes, and blood coagulation cascade proteins which have been incorporated into nanodiscs. We outline the advantages provided by homogeneity, ability to control oligomerization state of the target protein and lipid composition of the bilayer. Special attention is paid to the opportunities afforded by nanodisc system for the detailed studies of the role of different lipid properties and protein-lipid interactions in the functional behavior of membrane proteins.

Original languageEnglish (US)
Title of host publicationLipid-Protein Interactions
Subtitle of host publicationMethods and Protocols
PublisherHumana Press Inc.
Pages415-433
Number of pages19
ISBN (Print)9781627032742
DOIs
StatePublished - 2013
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume974
ISSN (Print)1064-3745

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Keywords

  • Cytochrome P450
  • GPCR
  • Lipid-protein interactions
  • Lipoproteins
  • Membrane protein solubilization
  • Nanodiscs
  • Tissue factor

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Schuler, M. A., Denisov, I. G., & Sligar, S. G. (2013). Nanodiscs as a new tool to examine lipid-protein interactions. In Lipid-Protein Interactions: Methods and Protocols (pp. 415-433). (Methods in Molecular Biology; Vol. 974). Humana Press Inc.. https://doi.org/10.1007/978-1-62703-275-9_18