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. Author manuscript; available in PMC: 2010 Dec 1.
Published in final edited form as: Nat Struct Mol Biol. 2010 May 30;17(6):768–774. doi: 10.1038/nsmb.1807

Figure 4.

Figure 4

Comparison of small bicelle versus micelle reconstitution of pSRII. (a) Overlay of [1H,15N]-TROSY correlation 2D spectra showing the backbone amide resonances of pSRII in DHPC micelles (cyan) and DMPC/c6-DHPC (q=0.3) small bicelles (red). (b) Chemical shift changes Δδ(1H,15N) = [(Δδ1H)2 + (Δδ 15N)2/6]0.5 in a are mapped onto the structure of pSRII. Increasingly larger differences are indicated by a gradual color change from blue to red as shown in the figure. The differences between micelle and small bicelle environments are generally small. Affected residues are located on the exterior of the protein mainly towards the helix extremities. (c) Overlay of 1H-1H cross-sections from 3D 15N-separated NOESY-HSQC spectra taken at the 15N frequencies of residues 97–101 for pSRII solubilized in either a micelle (blue) or small-bicelle (red) environment. Despite the chemical shift changes observed for these residues, the cross-peak pattern is unchanged indicating the preservation of the structural features. Sequential NOEs are annotated. The larger line width in the small bicelle spectra is due to the slower tumbling of the protein–bicelle complex.