Medical College of Wisconsin
CTSICores SearchResearch InformaticsREDCap

Nuclear magnetic resonance structural studies of membrane proteins in micelles and bilayers. Methods Mol Biol 2007;400:515-29

Date

10/24/2007

Pubmed ID

17951757

Pubmed Central ID

PMC2918260

DOI

10.1007/978-1-59745-519-0_35

Scopus ID

2-s2.0-36549056082 (requires institutional sign-in at Scopus site)   17 Citations

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.

Author List

Gong XM, Franzin CM, Thai K, Yu J, Marassi FM

Author

Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Gene Expression
Humans
Lipid Bilayers
Membrane Proteins
Micelles
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
Recombinant Proteins
Sodium-Potassium-Exchanging ATPase