Thesis final - after defense-7 - Jacobs University
Thesis final - after defense-7 - Jacobs University
Thesis final - after defense-7 - Jacobs University
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Chapter 3<br />
Figure 25 B: Represents the average polarity calculated by Zimmerman’s scale. The protein<br />
average polarity values of the three base supports were correlated with the respective salt<br />
concentrations where the fractions were collected. The error bars represent the standard<br />
deviations of the average polarity values in each fraction. The statistical analysis revealed a<br />
significant correlation (r 2 = 0.80; p < 0.0001).<br />
The r 2 values of the polarity with the retention of the proteins were 0.84 and 0.80 for the<br />
scales of Grantham and Zimmerman, respectively. An indirect relationship was also observed<br />
between polarity and flexibility of the proteins. The proteins with high polarity were less<br />
flexible and eluted at the beginning of the chromatography. These results confirmed the effect<br />
of average polarity in the chromatographic separation of proteins with the process proteomics<br />
approach. The polarity of the surface amino acids can also be used as an alternative parameter<br />
to average surface hydrophobicity and can be named as average surface polarity (ASP). The<br />
ASP parameter can be calculated for the tabulated proteins in the same way as ASH was<br />
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