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. Author manuscript; available in PMC: 2012 Nov 1.
Published in final edited form as: Nat Struct Mol Biol. 2011 Oct 16;18(11):1235–1243. doi: 10.1038/nsmb.2154

Figure 4. NMR characterization of the HxB2 MPER segment upon 2F5 Fab ligation.

Figure 4

(a) MPER backbone amide chemical shift changes upon binding to 2F5 Fab. The chemical shift values of both amide 15N and 1H are normalized as ((DH2 + (DN/5)2)1/2. (b) Secondary structures predicted from MPER chemical shifts by TALOS+. The red and light blue bars indicate probabilities of helical and beta-strand conformations respectively whereas grey bars represent unstructured regions. (c) Signal reduction observed in 2D-labeled MPER backbone amide peaks as transferred from 1H-saturated 2F5 Fab molecule to the MPER.