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. 2008 Feb 27;130(8):2400-1.
doi: 10.1021/ja711499r. Epub 2008 Feb 5.

Asymmetric methyl group labeling as a probe of membrane protein homo-oligomers by NMR spectroscopy

Nathaniel J Traaseth  1 , Raffaello Verardi, Gianluigi Veglia
Affiliations

Asymmetric methyl group labeling as a probe of membrane protein homo-oligomers by NMR spectroscopy

Nathaniel J Traaseth et al. J Am Chem Soc. .
No abstract available

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Figures

Figure 1
Figure 1
(A) Isotopic labeling scheme as shown on the pinwheel model of PLN. The red monomer of PLN is labeled [U-2H, 12C, 14N, 13CH3-Ileδ1], while the blue monomer is labeled [U-2H, 12C, 14N, 13CH3-Valγ1, 2, 13CH3-Leuδ1, 2]. Owing to the precursor chosen, only one of the methyl groups in the Val and Leu sample is 13CH3. Constant-time HSQC experiment on the 1/1 mixed sample showing Ileδ1 (red, B) and Valγ1, 2/Leuδ1, 2 (blue, C) methyl resonances.
Figure 2
Figure 2
Intermolecular NOEs detected for pentameric PLN. (A) 13C-ω1/1H-ω3 strip plots showing 13C-ω2 planes corresponding to L43d1, Ile45d1, and L43d2 (left to right). The green peaks are the intermolecular NOEs while the red and blue peaks are diagonal peaks. Dashed lines indicate connectivities between NOEs and diagonal peaks. (B) Overlap of 13C-ω2 planes for the Ile methyl region (12–14 ppm). The blue resonances are the same as in the Val/Leu HSQC shown in Figure 1a. Green peaks indicate all intermolecular NOEs from this experiment with a NOESY mixing time of 400 ms. Owing to the representation of ω2 overlap, several of the green peaks encompass more than one intermolecular NOE. The asterisks indicate NOEs with the DPC detergent.
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