Myoglobin Hill plot

Hill plots for myoglobin and hemoglobin are given in Figure 5-14. 

This means that the value of P50 may be determined from the Hill plot s y intercept or x inercept. For example, the y intercept in the case of myoglobin is 0, and since n = 1, = 1 mm Hg. For hemoglobin, the y intercept is -4.0. Using... 

Figure 7.6 Oxygen association with myoglobin (Mb) and human hemoglobin (Hb). (a) The Hill plot (b) a plot of oxygen partial pressure against the degree of hemoglobin saturation with oxygen.

Figure 8 Cooperative and noncooperative binding of O2. (a) Binding curves of myoglobin and hemoglobin, (b) Hill plot of binding curves. The Hill coefficient munber is determined from the first derivative (slope) of the HiU plots...

The Hill plot is obtained by plotting log([Mb02]/[Mb]) as a function of log[02]. For myoglobin this gives a straight line of slope equal to 1, the Hill coefficient (Fig. 6.8). 

Figure 7.9 Hill plots of oxygen binding for myoglobin and hemoglobin. 

Figure 1.3. A Hill plot of the set of designed elastic-contractile model proteins shown in Figure 1.2 with Hill coefficients, n, ranging from 1.5 to 8.0. B Hill plot of myoglobin (n = 1) and hemoglobin (n = 2.8). It is shown that the vaunted hemoglobin positive cooperativity is relatively small compared with that of designed elastic protein-based polymers and, in particular, of designed Model protein v.

FIGURE 14.6 Hill plots for the binding of oxygen to hemoglobin and myoglobin, is taken in mm Hg. 

The number of apparent binding sites for oxygen on a molecule of myoglobin or a molecule of hemoglobin may be determined with the aid of the linear form of the Hill Eq. (13.23). According to this equation, if log[17(l- Y)] is plotted versus log(pOa) a straight line is obtained with a slope equal to n, the number of apparent binding sites per molecule of protein (Fig. 7B). 

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