Myoglobin structure

FIGURE 16.2 Generalized myoglobin structure showing some amino acid units as open circles to illustrate the folded tertiary structure. 

Fig. 7. Microcalorimetric recording of the heat effect on cooling and subsequent heating of metmyoglobin solution at pH 3.83. The low temperature peaks correspond to heat release on cold denaturaton and heat absorption on subsequent renaturation of protein. The shift of these peaks in temperature is caused by slow kinetics of unfolding and folding of myoglobin structure at low temperature (for details, see Privalov et al 1986).

Figure 7.5 (a] Myoglobin structure (cartoon representation], its heme and two neighboring side chains (licorice], iron and the CO molecule (bulky], (b] Free energy profile of CO migration along two reaction coordinates linking different pockets DP — Xe4 and Xe4 -> Xe2. The two curves represent PC (red] and MTP (blue] electrostatics. See Ref [150] for more details. 

Q Would hydrophilic amino acids be found on the outside or inside of the myoglobin structure ... 

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