Team:WLC-Milwaukee/Modeling

From 2014.igem.org

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<p>DISCUSSION</p>
<p>DISCUSSION</p>
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</br></br></br></br></br></br></br></br>
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<h1>XynA at pH 8.8</h1>
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</br>
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<h2>2:1 Substrate-Enzyme Concentration</h2>
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<table border="1">
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<tr>
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  <td style="padding:5px" width="33%"><img src="https://static.igem.org/mediawiki/2014/1/10/XynA8.8_2E_1s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/1/17/XynA8.8_2E_5s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/0/01/XynA8.8_2E_15s.jpg"></td>
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</tr>
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</table>
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<p>As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.</p>
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</br>
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<h2>10:1 Substrate-Enzyme Concentration</h2>
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<table border="1">
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<tr>
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  <td style="padding:5px" width="33%"><img src="https://static.igem.org/mediawiki/2014/6/67/XynA8.8_10E_1s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/6/66/XynA8.8_10E_5s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/7/74/XynA8.8_10E_15s.jpg"></td>
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</tr>
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</table>
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<p>As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.</p>
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 +
</br>
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 +
<h2>100:1 Substrate-Enzyme Concentration</h2>
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 +
<table border="1">
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<tr>
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  <td style="padding:5px" width="33%"><img src="https://static.igem.org/mediawiki/2014/7/7b/XynA8.8_100E_1s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src=" https://static.igem.org/mediawiki/2014/8/8d/XynA8.8_100E_5s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/b/b6/XynA8.8_100E_15s.jpg"></td>
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</tr>
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</table>
 +
 +
<p>As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.</p>
 +
 +
</br>
 +
 +
<h2>Increased Substrate Concentration at 15 Seconds</h2>
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 +
<table border="1">
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<tr>
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  <td style="padding:5px" width="33%"><img src=" https://static.igem.org/mediawiki/2014/0/01/XynA8.8_2E_15s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/7/74/XynA8.8_10E_15s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/b/b6/XynA8.8_100E_15s.jpg"></td>
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</tr>
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</table>
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<p>Despite the increase in substrate concentration with a constant enzyme concentration, all substrate was catalyzed into product in similar amounts of time.</p>
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</br>
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<p>DISCUSSION</p>
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</br></br></br></br></br></br></br></br></br></br>
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<h1>YesZ at pH 7.0</h1>
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</br>
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<h2>2:1 Substrate-Enzyme Concentration</h2>
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 +
<table border="1">
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<tr>
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  <td style="padding:5px" width="33%"><img src="https://static.igem.org/mediawiki/2014/5/55/YesZ_2E_1s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/0/04/YesZ_2E_5s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/7/7d/YesZ_2E_15s.jpg"></td>
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</tr>
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</table>
 +
 +
<p>As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.</p>
 +
 +
</br>
 +
 +
<h2>10:1 Substrate-Enzyme Concentration</h2>
 +
 +
<table border="1">
 +
<tr>
 +
  <td style="padding:5px" width="33%"><img src="https://static.igem.org/mediawiki/2014/7/77/YesZ_10E_1s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/2/25/YesZ_10E_5s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/4/4d/YesZ_10E_15s.jpg"></td>
 +
</tr>
 +
</table>
 +
 +
<p>As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.</p>
 +
 +
</br>
 +
 +
<h2>100:1 Substrate-Enzyme Concentration</h2>
 +
 +
<table border="1">
 +
<tr>
 +
  <td style="padding:5px" width="33%"><img src="https://static.igem.org/mediawiki/2014/0/08/YesZ_100E_1s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/1/12/YesZ_100E_5s.jpg"></td>
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  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/8/8f/YesZ_100E_15s.jpg"></td>
 +
</tr>
 +
</table>
 +
 +
<p>As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.</p>
 +
 +
</br>
 +
 +
<h2>Increased Substrate Concentration at 15 Seconds</h2>
 +
 +
<table border="1">
 +
<tr>
 +
  <td style="padding:5px" width="33%"><img src="https://static.igem.org/mediawiki/2014/7/7d/YesZ_2E_15s.jpg"></td>
 +
  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/4/4d/YesZ_10E_15s.jpg"></td>
 +
  <td style="padding:5px" width="33%"><img  src="https://static.igem.org/mediawiki/2014/8/8f/YesZ_100E_15s.jpg"></td>
 +
</tr>
 +
</table>
 +
 +
<p>Despite the increase in substrate concentration with a constant enzyme concentration, all substrate was catalyzed into product in similar amounts of time.</p>
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</br>
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<p>DISCUSSION</p>
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</html>
</html>

Revision as of 06:42, 17 October 2014


This code models Michaelis-Menten enzyme kinetics over a user inputted time duration. Product formation and enzyme-substrate complex formation are assumed irreversible. Initial concentrations of the E-S complex and product are assumed to be zero. And it does not account for the presence of inhibitors or activators. Using the law of mass action the enzyme substrate complex, and product formation chemical equations, are separated into a set of differential equations. The MATLAB ode45 function is used to solve the set of differential equations over the given time span.

XynA at pH 7.3


2:1 Substrate-Enzyme Concentration

As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.


10:1 Substrate-Enzyme Concentration

As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.


100:1 Substrate-Enzyme Concentration

As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.


Increased Substrate Concentration at 15 Seconds

Despite the increase in substrate concentration with a constant enzyme concentration, all substrate was catalyzed into product in similar amounts of time.


DISCUSSION









XynA at pH 8.8


2:1 Substrate-Enzyme Concentration

As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.


10:1 Substrate-Enzyme Concentration

As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.


100:1 Substrate-Enzyme Concentration

As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.


Increased Substrate Concentration at 15 Seconds

Despite the increase in substrate concentration with a constant enzyme concentration, all substrate was catalyzed into product in similar amounts of time.


DISCUSSION











YesZ at pH 7.0


2:1 Substrate-Enzyme Concentration

As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.


10:1 Substrate-Enzyme Concentration

As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.


100:1 Substrate-Enzyme Concentration

As time progresses from 1 second to 15 seconds, the reaction moves to completion and almost all substrate has been catalyzed into product.


Increased Substrate Concentration at 15 Seconds

Despite the increase in substrate concentration with a constant enzyme concentration, all substrate was catalyzed into product in similar amounts of time.


DISCUSSION

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