Sperm whale apoMb

Fig. 17. (A) The high-frequency shifted portion of the 400 MHz H NMR spectrum of sperm whale apoMb in 90%H20/10% H20, pH 8.55, at 5 °C. Peaks a c are resolved below 11 ppm. (B) The NOE difference spectrum resulting from saturation of peak a. The peaks at 6.66 and 7.83 ppm exhibit NOEs. (C) The NOE difference spectrum resulting from saturation of peak b. The peaks at 6.81 and 7.68 ppm exhibit NOEs. (D) The NOE difference spectrum resulting from saturation of peak c. The peak at 7.76 ppm exhibits an NOE. The signal assignments are indicated in traces B—D. (From ref. 187, with permission from Elsevier Science.)...

Table 3. Chemical shifts (ppm) of HisEFS imidazole ring NH proton signals of sperm whale apoMb and reconstituted Mbs at 5 °C...

Figure 35. Global mapping of surface hydration dynamics of apoMb. Shown is the X-ray crystal structure of sperm whale myoglobin (PDB ID 1MBD) in the holo form with eight helices A—H. In apo form, parts of the structure are melted and they are shown in transparent gray. The 16 balls indicate positions of mutation with tryptophan one at a time.

Fig. 18. The high-frequency shifted portions of the 400 MHz H NMR spectra of sperm whale metMb(OH ) and apoMb in 90%H20/10%-H20 at 5 °C and neutral (left) and basic (right) pH values. Peak indicated by an asterisk is due to impurity. The preparation of apoMb from Mb is schematically represented in the inset.

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