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Additional file 7: Figure S6. Prediction performance of oxy-90 models. Prediction performance of the developed models on oxy-class of protein sequences. E-1, E-2, E-3, E-4, E-5 and E-6 of Ery, Hcy, Heme, Hemo, Leg and Myo models performance in AC approach. F-1, F-2, F-3, F-4, F-5 and F-6 of Ery, Hcy, Heme, Hemo, Leg and Myo models performance in DC approach. G-1, G-2, G-3, G-4, G-5 and G-6 of Ery, Hcy, Heme, Hemo, Leg and Myo models performance in PSSM approach. H-1, H-2, H-3, H-4, H-5 and H-6 of Ery, Hcy, Heme, Hemo, Leg and Myo models performance in the hybrid approach. The X-axis is indexed on oxy-class proteins (Ery, Hcy, Heme, Hemo, Leg and Myo) and the Y-axis is the SVM model prediction scores

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Additional file 3: Figure S3. Sequence length profile oxy-classes. Sequence length range in histogram based on oxy-subclass organizations. X-axis for sequence length range and Y-axis for number of sequences

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Additional file 1: Figure S1. Amino acid distribution chart of oxy-proteins along with non-oxy, difference between 50 and 90 data

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Additional file 6: Figure S5. Prediction performance of oxy-50 models. Prediction performance of the developed models on oxy-class of protein sequences. A-1, A-2, A-3, A-4, A-5 and A-6 of Ery, Hcy, Heme, Hemo, Leg and Myo models performance in AC approach. B-1, B2, B-3, B-4, B-5 and B-6 of Ery, Hcy, Heme, Hemo, Leg and Myo models performance in DC approach. C-1, C-2, C-3, C-4, C-5 and C-6 of Ery, Hcy, Heme, Hemo, Leg and Myo models performance in PSSM approach. D-1, D-2, D-3, D-4, D-5 and D-6 of Ery, Hcy, Heme, Hemo, Leg and Myo models performance in the hybrid approach. The X-axis is indexed on oxy-class proteins (Ery, Hcy, Heme, Hemo, Leg and Myo) and the Y-axis is the SVM model prediction scores

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Additional file 5: Figure S4. ROC curve oxy-non-oxy in all approaches. The performance of oxypred2 models by receiver operating characteristic (ROC) plots in all approaches. The area under curve (AUC) was measured for all developed models. It is mainly to show the relationship between sensitivity and 1-specificity for each thresholds of the real value out-puts

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Additional file 9: Figure S8. Average Acc, Sen and Sep from 1.5 to -1.5 thresholds, performance compared both oxy-50 and oxy-90 datasets

Fractions of each type of secondary structure in lipase covalently immobilised to amino-functionalised MWNT.

<p>Abbreviations: H(r), regular α-helix; H(d), distorted α-helix; S(r), regular β sheet; s(d), distorted β sheet; Trn, Turn; Unrd, unordered. All experiments in this study were carried out in triplicate with standard deviation below 5%.</p

Thermal gravimetric analysis (TGA) plot for pristine MWNT and amino-functionalised MWNT.

<p>Thermal gravimetric analysis (TGA) plot for pristine MWNT and amino-functionalised MWNT.</p

Reusability study of the immobilised lipase.

<p>Footnote: The lipolytic activity was determined following the method of Winkler and Stuckmann <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0073642#pone.0073642-Boncel1" target="_blank">[21]</a>, using p-NP palmitate as substrate. Bars indicate the standard deviation from triplicate determinations. Residual activity of immobilised enzyme at different cycles. 1 cycle = 100±4.2; 2 cycle = 88±3.9; 3 cycle = 84±4.0; 4 cycle = 80±2.9; 5 cycle = 70±3.0; 6 cycle = 64±4.4; 7 cycle = 62±3.9; 8 cycle = 56±4.5; 9 cycle = 54±4.8; 10 cycle = 51±4.3; 11 cycle = 49±4.2.</p

a) XPS spectrum of MWNT and MWNT bound lipase showing carbon 1 s high resolution spectra. b) XPS spectrum of MWNT and MWNT bound lipase showing nitrogen 1 s high resolution spectra.

<p>a) XPS spectrum of MWNT and MWNT bound lipase showing carbon 1 s high resolution spectra. b) XPS spectrum of MWNT and MWNT bound lipase showing nitrogen 1 s high resolution spectra.</p