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. 2020 Jul 22;21(21):3087–3095. doi: 10.1002/cbic.202000348

Figure 1.

Figure 1

Top: amino acid sequence of p53TAD1–60, boxes represent the regions undergoing structural changes. A) 1H,15N HSQC spectra at 313 K and 700 MHz of 15N‐labeled p53TAD1–60 (black) and p53TAD1–60 in complex with unlabeled, Ca2+‐loaded S100A4 (red, with assignment). B) Binding information: cumulative Δδ chemical shift changes of p53TAD1–60 resonances upon S100A4 binding. Residues broadened below the detection limit are represented by an asterisk. C) Structural information: secondary structure propensities (SSP) for free (black) and complexed (red) p53TAD1–60. D) Backbone dynamics results: reduced spectral density mapping J(ωN) vs J(0) for free (black) and complexed p53TAD1–60 (red).