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Team:WLC-Milwaukee/Modeling
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<h1>Protein Modeling</h1> | <h1>Protein Modeling</h1> | ||
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. | 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. | ||
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Revision as of 17:06, 17 October 2014
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Protein Modeling
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. INPUT CODE AND DATA???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
