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Figure 3
NMR spectral change of uniformly 15N-labeled αSN upon interaction with the PbaB tetramer. (a) Superimposed 1H-15N HSQC spectra of uniformly 15N-labeled αSN in the absence (black) and presence (red) of PbaB. (b) Intensity ratio plots of the backbone amide peaks of αSN upon interaction with PbaB. Asterisks indicate the amino acid residues whose peaks were unobservable in the spectrum or whose chemical shift perturbation data were obscured by severe peak overlapping, while P denotes the proline residues.

Journal logoJOURNAL OF
APPLIED
CRYSTALLOGRAPHY
ISSN: 1600-5767
Volume 47| Part 1| February 2014| Pages 430-435
doi:10.1107/S1600576713033475
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