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 16 B: Represents the average polarity calculated by Zimmerman’s scale. The protein<br />
average polarity values of the three ligands 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 = 0.76; p < 0.0001).<br />
This revealed that proteins with high polar residues in the protein sequence were eluted at<br />
high salt concentrations at the beginning of the chromatography. In contrast, the proteins with<br />
less polar residues in the protein sequence were eluted at the end of the chromatography at<br />
low salt concentrations. The polar residues are usually the acidic and basic amino acids (Asp,<br />
Asn, Glu, Lys, Arg, Gln). These amino acid residues are highly polar and occur on the surface<br />
of protein at an aqueous interface. The non-polar residues such as (Ala, Val, Leu, Ile, Cys,<br />
Met, Pro, Phe, and Trp) are usually found in the interior portion of the proteins (117). Based<br />
on the abundance of these residues in a protein sequence, the polarity value has been assigned.<br />
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