Nuclear magnetic resonance structural studies of membrane proteins in micelles and bilayers

Methods Mol Biol. 2007:400:515-29. doi: 10.1007/978-1-59745-519-0_35.

Abstract

Nuclear magnetic resonance (NMR) spectroscopy enables determination of membrane protein structures in lipid environments, such as micelles and bilayers. This chapter outlines the steps for membrane-protein structure determination using solution NMR with micelle samples, and solid-state NMR with oriented lipid-bilayer samples. The methods for protein expression and purification, sample preparation, and NMR experiments are described and illustrated with examples from gamma and CHIF, two membrane proteins that function as regulatory subunits of the Na+- and K+-ATPase.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Gene Expression
  • Humans
  • Lipid Bilayers / chemistry*
  • Membrane Proteins / chemistry*
  • Micelles*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Sodium-Potassium-Exchanging ATPase / biosynthesis
  • Sodium-Potassium-Exchanging ATPase / chemistry*
  • Sodium-Potassium-Exchanging ATPase / isolation & purification

Substances

  • Lipid Bilayers
  • Membrane Proteins
  • Micelles
  • Recombinant Proteins
  • corticosteroid hormone-induced factor
  • Sodium-Potassium-Exchanging ATPase