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Fig. 7. (A,C) The H{alpha} CSDs for synthetic peptides with (A) 679-LL or (C) 679-AA sequences where a value of 0 corresponds to random coil. CSDs are represented as ppm on the x-axis [ppm=(shift observed/oscillator frequency)x106]. Positive and negative values represent upfield and downfield shifts, respectively. Amino acid residues are labeled on the y-axis, based on the published human EGFR sequence (NCBI accession number P00533). Data were obtained for peptides dissolved in water (open bars) or in the presence of DPC micelles (black bars) at 5°C. (B,D) Summary of intramolecular NOEs observed for (B) wild-type and (D) mutant peptides in the presence of DPC micelles. NOE-intensity-strength is indicated by the thickness of the lines. Dotted lines indicate proline C{delta}H-proton resonance effects.





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