Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments are combined with novel through-bond correlation schemes that probe mobile protein segments. These NMR schemes are demonstrated on a uniformly [13C,15N] variant of the 52-residue polypeptide phospholamban. When reconstituted in lipid bilayers, the NMR data are consistent with an alpha-helical trans-membrane segment and a cytoplasmic domain that exhibits a high degree of structural disorder.
Andronesi
Ovidiu C
OC
Department of NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Becker
Stefan
S
Seidel
Karsten
K
Heise
Henrike
H
Young
Howard S
HS
Baldus
Marc
M
D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017433:Protein Structure, Secondary; D012680:Sensitivity and Specificity; D013113:Spin Labels; D013816:Thermodynamics; D000099211:Phospholamban
D002135:Calcium-Binding Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D013113:Spin Labels; D000099211:Phospholamban