Figure 3.

NMR chemical shift data. Top: secondary structure of Bet v 1.0101 as defined by Gajhede et al. (14). Middle: TALOS+ secondary structure probabilities (blue, β-sheet; red, α-helix) of Bet v 1.0101 derived from ¹H^N, ¹⁵N, ¹³C’, ¹³C^α, and ¹³C^β chemical shifts for the apo protein compared with complexes with SDS and STS. For residues that are marked by an asterisk, resonance assignments were not obtained. Bottom: cumulative chemical shift differences, Δω_cum, between Bet v 1.0101 in the absence of ligand and Bet v 1.0101 in complex with SDS (blue) and STS (red), respectively, as a function of residue number. To see this figure in color, go online.