Heteronuclear 2D-correlations in a uniformly [13C, 15N] labeled membrane-protein complex at ultra-high magnetic fields.
One- and two-dimensional solid-state NMR experiments on a uniformly labeled intrinsic membrane-protein complex at ultra-high magnetic fields are presented. Two-dimensional backbone and side-chain correlations for a [U-13C, 15N] labeled version of the LH2 light-harvesting complex indicate significant resolution at low temperatures and under Magic Angle Spinning. Tentative assignments of some of the observed correlations are presented and attributed to the alpha-helical segments of the protein, mostly found in the membrane interior.
Egorova-Zachernyuk
T A
TA
Gorlaeus Laboratories, Leiden University, The Netherlands.
Hollander
J
J
Fraser
N
N
Gast
P
P
Hoff
A J
AJ
Cogdell
R
R
de Groot
H J
HJ
Baldus
M
M
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D003080:Cold Temperature; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D012680:Sensitivity and Specificity
D002247:Carbon Isotopes; D008565:Membrane Proteins; D009587:Nitrogen Isotopes; D045322:Photosynthetic Reaction Center Complex Proteins