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The horizontal bars represent the aliphatic index of each sequence.
The aliphatic index and grand average of hydropathicity were 154.71 and 0.106.
The aliphatic index is regarded as a positive factor for the increased thermostability of globular proteins (Ikai 1980).
Thermostability, measured according to the aliphatic index, showed higher values for certain homologs compared with their mesophilic relatives.
All those homologs which showed an aliphatic index ≥80.88 are indicated by an arrow, while clades representing only the thermophilic homologs are denoted by asterisks.
For each protein, the aliphatic index (relative volume occupied by aliphatic side chains) (Ikai 1980) was calculated using ProtParam (Gasteiger et al. 2005).
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Blue and orange vertical dotted lines indicate the average aliphatic indices obtained for mesophilic (75.25) and thermophilic (80.88) RO homologs, respectively.
The average length, weight, isoelectric point, and aliphatic indices of the proteins were 322.4 ± 209.9, 36.2 ± 24.9, 7.2.4 ± 1.7, and 97.9 ± 15.2 (mean ± standard deviation [SD]), respectively.
The aliphatic indices for the two proteins were 84.14 (HsHDR1) and 82.06 (HsHDR2), and the grand averages of hydropathicity were −0.330 (HsHDR1) and −0.363 (HsHDR2) (Table 3).
In addition, the aliphatic and the instability index of the protein described it as an aliphatic and stable protein, respectively.
Horizontal flows of two initially stratified immiscible liquids with matched refractive indices, namely an aliphatic hydrocarbon oil (Exxsol D80) and an aqueous-glycerol solution, are investigated by combining two laser-based optical-diagnostic measurement techniques.
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