Nuclear magnetic resonance structural studies of membrane proteins in micelles and bilayers.
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.
Gong
Xiao-Min
XM
The Burnham Institute, La Jolla, CA, USA.
Franzin
Carla M
CM
Thai
Khang
K
Yu
Jinghua
J
Marassi
Francesca M
FM
D000818:Animals; D015870:Gene Expression; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D008823:Micelles; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D000254:Sodium-Potassium-Exchanging ATPase / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification
D008051:Lipid Bilayers; D008565:Membrane Proteins; D008823:Micelles; D011994:Recombinant Proteins; C422209:corticosteroid hormone-induced factor; D000254:Sodium-Potassium-Exchanging ATPase