Thesis final - after defense-7 - Jacobs University

Chapter 3
Figure 24 C: Represents the average hydrophobicity calculated by the scale of Tanford. The
protein average hydrophobicity values of the three base supports were correlated with the
respective salt concentrations where the fractions were collected. The error bars represent the
standard deviations of the average hydrophobicity values in each fraction. The statistical
analysis revealed a significant correlation (r 2 = 0.79; p < 0.0001).
It was reported that the folded proteins have less non polar surface area in comparison to the
unfolded ones (125). This confirmed that during unfolding, the hydrophobic residues of the
proteins were exposed on the surface and resulted in longer retention during chromatography.
It was also described in the mentioned report that there has been no relation to the non-polar
surface area and the size of protein. In the same way, no relation was observed here between
the size and hydrophobicity of the proteins. It has been reported that there were very few
buried residues which have zero accessible surface area. Most of the protein interior was
composed of amino acids have contact with the solvent (125). This also revealed that most of
88