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− | <h2 class="content-1" id="titleL" style="color:# | + | <h2 class="content-1" id="titleL" style="color:#FFBB66">I. Summary</h2> |
<div class="modelingPartContent" id="partL"> | <div class="modelingPartContent" id="partL"> | ||
<p class="content">The aim of this modeling was to predict and simulate the degradation rate of Pantide. Practically, the results would be integrated into our device to promote automatic control system. Once Pantide degraded below the effective level, it will spray the solution to replenish.</p> | <p class="content">The aim of this modeling was to predict and simulate the degradation rate of Pantide. Practically, the results would be integrated into our device to promote automatic control system. Once Pantide degraded below the effective level, it will spray the solution to replenish.</p> | ||
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− | <h2 class="content-1" id="titleM" style="color:# | + | <h2 class="content-1" id="titleM" style="color:#FFBB66">II. Pantide degradation process</h2> |
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<p class="content">For the proteins used as Pantide, the inhibitor cystine knot (ICK) is significant to their function. Pantide with several disulfide bonds is often more stable in solution. If “native protein” is denatured, it loses disulfide bonds and becomes a less stable form, normally called “linear protein,” which is easily degradable.</p> | <p class="content">For the proteins used as Pantide, the inhibitor cystine knot (ICK) is significant to their function. Pantide with several disulfide bonds is often more stable in solution. If “native protein” is denatured, it loses disulfide bonds and becomes a less stable form, normally called “linear protein,” which is easily degradable.</p> | ||
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<p class="content">There are many possible processes of Pantide degradation we discussed below. (Figure 1) Pantide may have a chance to be reduced to a linear form by reductants or reductases. For both native form and linear form proteins, it may suffer hydrolysis and proteolysis, resulting in denaturing or amino acid cleavage. Also, UV light of sun also leads to Pantide degradation. Though the energy of UV light may not be not enough to break the covalent bonds efficiently, proteins still could undergo radiolytic oxidation.</p> | <p class="content">There are many possible processes of Pantide degradation we discussed below. (Figure 1) Pantide may have a chance to be reduced to a linear form by reductants or reductases. For both native form and linear form proteins, it may suffer hydrolysis and proteolysis, resulting in denaturing or amino acid cleavage. Also, UV light of sun also leads to Pantide degradation. Though the energy of UV light may not be not enough to break the covalent bonds efficiently, proteins still could undergo radiolytic oxidation.</p> | ||
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− | <img src="https://static.igem.org/mediawiki/2016/5/5e/NCTU_F1.png" class="picture" style="width: | + | <img src="https://static.igem.org/mediawiki/2016/5/5e/NCTU_F1.png" class="picture" style="width:80%;left:8vw"> |
<p class="content-image" style="text-align:center !important;">Figure 1. Pantide degradation process</p> | <p class="content-image" style="text-align:center !important;">Figure 1. Pantide degradation process</p> | ||
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− | <h2 class="content-1" id="titleN" style="color:# | + | <h2 class="content-1" id="titleN" style="color:#FFBB66">III. Hydrolysis test</h2> |
<div class="modelingPartContent" id="partN"> | <div class="modelingPartContent" id="partN"> | ||
<p class="content-1" style="color:#00E600"> i. Theory</p> | <p class="content-1" style="color:#00E600"> i. Theory</p> | ||
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− | <h2 class="content-1" id="titleO" style="color:# | + | <h2 class="content-1" id="titleO" style="color:#FFBB66">IV. Proteolysis test</h2> |
<div class="modelingPartContent" id="partO"> | <div class="modelingPartContent" id="partO"> | ||
<p class="content-1" style="color:#00E600"> i. Theory</p> | <p class="content-1" style="color:#00E600"> i. Theory</p> | ||
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− | <img src="https://static.igem.org/mediawiki/2016/f/fb/F6.png" class="picture" style="width: | + | <img src="https://static.igem.org/mediawiki/2016/f/fb/F6.png" class="picture" style="width:80%;left:8vw"> |
<p class="content-image" style="text-align:center !important;">Figure 6. Lineweaver–Burk plot of proteolysis test of linear Hv1a (blue line) and Hv1a-lectin (orange line). The horizontal axis represents the reciprocal of substrate concentration, and the longitudinal axis represents the reciprocal of rate. The straight line’s x-intercept means the reciprocal of <i>-K<sub>M,p </sub></i>, and y-intercept means the reciprocal of <i>V<sub>m,p</sub> </i>.</p> | <p class="content-image" style="text-align:center !important;">Figure 6. Lineweaver–Burk plot of proteolysis test of linear Hv1a (blue line) and Hv1a-lectin (orange line). The horizontal axis represents the reciprocal of substrate concentration, and the longitudinal axis represents the reciprocal of rate. The straight line’s x-intercept means the reciprocal of <i>-K<sub>M,p </sub></i>, and y-intercept means the reciprocal of <i>V<sub>m,p</sub> </i>.</p> | ||
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− | <h2 class="content-1" id="titleP" style="color:# | + | <h2 class="content-1" id="titleP" style="color:#FFBB66">V. UV radiolytic oxidation test</h2> |
<div class="modelingPartContent" id="partP"> | <div class="modelingPartContent" id="partP"> | ||
<p class="content-1" style="color:#00E600"> i. Theory</p> | <p class="content-1" style="color:#00E600"> i. Theory</p> | ||
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<p class="content">Ionizing radiation causes the radiolysis of water is, the major process is shown below. (Figure 7)</p> | <p class="content">Ionizing radiation causes the radiolysis of water is, the major process is shown below. (Figure 7)</p> | ||
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− | <img src="https://static.igem.org/mediawiki/2016/a/ac/NCTU_F7.png" class="picture" style="width: | + | <img src="https://static.igem.org/mediawiki/2016/a/ac/NCTU_F7.png" class="picture" style="width:60%;left:8vw"> |
<p class="content-image" style="text-align:center !important;">Figure 7. The radiolysis process of water.</p> | <p class="content-image" style="text-align:center !important;">Figure 7. The radiolysis process of water.</p> | ||
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<p class="content">We then used software MATLAB to simulate the degradation rate by UV radiolytic oxidation on the intensity of UVB from sunlight. The results showed that the degradation rate increases as rising intensity whatever n is, and eventually it tends to be fully degraded. (Figure 8)</p> | <p class="content">We then used software MATLAB to simulate the degradation rate by UV radiolytic oxidation on the intensity of UVB from sunlight. The results showed that the degradation rate increases as rising intensity whatever n is, and eventually it tends to be fully degraded. (Figure 8)</p> | ||
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− | <img src="https://static.igem.org/mediawiki/2016/8/87/F8.png" class="picture" style="width: | + | <img src="https://static.igem.org/mediawiki/2016/8/87/F8.png" class="picture" style="width:100%;left:8vw"> |
<p class="content-image" style="text-align:center !important;">Figure 8. The simulation of degradation rate by UV radiolytic oxidation on the intensity of UVB from sunlight.</p> | <p class="content-image" style="text-align:center !important;">Figure 8. The simulation of degradation rate by UV radiolytic oxidation on the intensity of UVB from sunlight.</p> | ||
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− | <h2 class="content-1" id="titleQ" style="color:# | + | <h2 class="content-1" id="titleQ" style="color:#FFBB66">VI. Summarization</h2> |
<div class="modelingPartContent" id="partQ"> | <div class="modelingPartContent" id="partQ"> | ||
<p class="content">The whole equation of degradation rate could be expressed by the summation of the rates of three possible degrade processes, that is hydrolysis, proteolysis, and UV radiolytic oxidation, and the rate that proteins transfer from native form to linear form indicated as <i>R<sub>SS </sub></i></p> | <p class="content">The whole equation of degradation rate could be expressed by the summation of the rates of three possible degrade processes, that is hydrolysis, proteolysis, and UV radiolytic oxidation, and the rate that proteins transfer from native form to linear form indicated as <i>R<sub>SS </sub></i></p> | ||
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− | <h2 class="content-1" id="titleR" style="color:# | + | <h2 class="content-1" id="titleR" style="color:#FFBB66">Reference</h2> |
<div class="modelingPartContent" id="partR"> | <div class="modelingPartContent" id="partR"> | ||
<p class="reference-content">[1] Volker Herzig and Glenn F. King (2015). The Cystine Knot Is Responsible for the Exceptional Stability of the Insecticidal Spider Toxin ω-Hexatoxin-Hv1a. Toxins, 7, 4366-4380.</p> | <p class="reference-content">[1] Volker Herzig and Glenn F. King (2015). The Cystine Knot Is Responsible for the Exceptional Stability of the Insecticidal Spider Toxin ω-Hexatoxin-Hv1a. Toxins, 7, 4366-4380.</p> |
Latest revision as of 03:04, 4 November 2016