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. 2015 Sep 24;10(9):e0137973. doi: 10.1371/journal.pone.0137973

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Fig 5 — The polarity (A, D, G), the optimized matching hydrophobicity (B, E, H), and hydropathicity (C, F, I) plots of the wild-type and mutant CRYAB proteins. Both mutant proteins (R11C and R12C) revealed low polarity (compare A, with D and G), a higher hydrophobicity (compare B, with E and H), and higher hydropathicity (compare C, with F and I), respectively. The x-axis represents the position of amino acids. The y-axis represents the Polarity, hydrophobicity and Hydropathicity values in a default window size of 9. The arrows point to the difference in their respective polarities (1^st arrow from the left), hydrophobicity (2^nd arrow from the left) and hydropathicities (3^rd arrow from the left).