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Thesis final - after defense-7 - Jacobs University

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Chapter 3<br />

proteins with medium or high ASH values. The proteins were classified into three groups such<br />

as low, medium or highly hydrophobic, depending on the ASH and the corresponding salt<br />

concentrations on which the proteins were eluted during chromatography. The proteins eluted<br />

at high salt concentrations in the beginning of the chromatography were grouped as less<br />

hydrophobic than those proteins eluted at the middle and / or at the end of the<br />

chromatography.<br />

Figure 19: Represents the average surface hydrophobicity calculated by Cowan-Whittaker’s<br />

scale. The protein average surface hydrophobicity values of the three ligands were correlated<br />

with the respective salt concentrations where the fractions were collected. The error bars<br />

represent the standard deviations of the average surface hydrophobicity values in each<br />

fraction. The statistical analysis on average revealed a significant correlation (r 2 = 0.90; p <<br />

0.006).<br />

The ASH values were 0.413, 0.458 and 0.522 for the proteins eluted at the beginning, middle<br />

and at the end of the chromatography, respectively. These ranges were in agreement of the<br />

67

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