Assigning solid-state NMR spectra of aligned proteins using isotropic chemical shifts.
A method for assigning solid-state NMR spectra of membrane proteins aligned in phospholipid bicelles that makes use of isotropic chemical shift frequencies and assignments is demonstrated. The resonance assignments are based on comparisons of 15N chemical shift differences in spectra obtained from samples with their bilayer normals aligned perpendicular and parallel to the direction of the applied magnetic field.
De Angelis
Anna A
AA
Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, 0307 La Jolla, CA 92093-0307, USA.
Howell
Stanley C
SC
Opella
Stanley J
SJ
D000465:Algorithms; D016880:Anisotropy; D008051:Lipid Bilayers / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000032:analysis* / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D011487:Protein Conformation
D008051:Lipid Bilayers; D008565:Membrane Proteins; D010743:Phospholipids