DataExtract

data extract of 'Software Change Proneness Prediction Through Combination of Bagging and Re-sampling Methods

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The data of 'Software Change Proneness Prediction Through Combination of Bagging and Re-sampling Methods

Change Prone Prediction

Source files of 'Software Change Proneness Prediction Through Combination of Bagging and Re-sampling Methods

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Data and source code and some .sh files for data extract of manuscript entitled 'Software Change Proneness Prediction Through Combination of Bagging and Re-sampling Methods

SDS-PAGE analysis of Recombinant <i>Tm</i>Cel12B.

<p>Lane M, Protein marker; Lane 1, Supernatant after ultrosonication; Lane 2, suspensions after ammonium sulfate precipitation; Lane 3, treated by heat at 75°C for 15 min; Lane 4, purified enzyme after purification kit.</p

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<p>The vertex and graph both occurred in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0097178#pone-0097178-g001" target="_blank">Figure 1</a>.</p

Site-Directed Mutagenesis of a Hyperthermophilic Endoglucanase Cel12B from <i>Thermotoga maritima</i> Based on Rational Design

<div><p>To meet the demand for the application of high activity and thermostable cellulases in the production of new-generation bioethanol from nongrain-cellulose sources, a hyperthermostable β-1,4-endoglucase Cel12B from <i>Thermotoga maritima</i> was selected for further modification by gene site-directed mutagenesis method in the present study, based on homology modeling and rational design. As a result, two recombinant enzymes showed significant improvement in enzyme activity by 77% and 87%, respectively, higher than the parental enzyme <i>Tm</i>Cel12B. Furthermore, the two mutants could retain 80% and 90.5% of their initial activity after incubation at 80°C for 8 h, while only 45% for 5 h to <i>Tm</i>Cel12B. The <i>K</i>_m and <i>V</i>_max of the two recombinant enzymes were 1.97±0.05 mM, 4.23±0.15 μmol·mg^-1·min^-1 of <i>Tm</i>Cel12B-E225H-K207G-D37V, and 2.97±0.12 mM, 3.15±0.21 μmol·mg^-1·min^-1 of <i>Tm</i>Cel12B-E225H-K207G, respectively, when using CMC-Na as the substrate. The roles of the mutation sites were also analyzed and evaluated in terms of electron density, hydrophobicity of the modeled protein structures. The recombinant enzymes may be used in the hydrolysis of cellulose at higher temperature in the future. It was concluded that the gene mutagenesis approach of a certain active residues may effectively improve the performance of cellulases for the industrial applications and contribute to the study the thermostable mechanism of thermophilic enzymes.</p></div

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<p>All of () are combined to the .</p

Structures of site-directed amino acid residues with other vicinal residues by H-bond.

<p>A, B: Glutamic acid 225 was mutated into Histidine. C, D: Aspartic acid 37 was mutated into Valine. E, F: Lysine 207 was mutated into Glutamic acid.</p

A Filtering Example.

<p>For the labeled graphs and , (a) lists the of all vertices in and ; (b) lists the candidate vertices set for each vertex in .</p