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The elements of the rate vector will be rate equations that are functions of one or more species and parameters, p. In the example, these might be simple mass-action rate laws such as = where is the rate constant parameter. The particular laws chosen will depend on the specific system under study.
The product itself depends on the purpose of the model, but one of the most common examples is the study of total biomass. A notable example of the success of FBA is the ability to accurately predict the growth rate of the prokaryote E. coli when cultured in different conditions. [10]
In biochemistry and in biological fluids, at pH = 7, it is thus important to note that the reduction potential of the protons ( H +) into hydrogen gas H 2 is no longer zero as with the standard hydrogen electrode (SHE) at 1 M H + (pH = 0) in classical electrochemistry, but that E red = − 0.414 V {\displaystyle E_{\text{red}}=-0.414\mathrm {V ...
It is possible to build a computer simulation of a linear biochemical pathway. This can be done by building a simple model that describes each intermediate through a differential equation. The differential equations can be written by invoking mass conservation. For example, for the linear pathway:
The solution of the equations, by either analytical or numerical means, describes how the biological system behaves either over time or at equilibrium. There are many different types of equations and the type of behavior that can occur is dependent on both the model and the equations used. The model often makes assumptions about the system.
Curve of the Michaelis–Menten equation labelled in accordance with IUBMB recommendations. In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product.
The Hill equation is used extensively in pharmacology to quantify the functional parameters of a drug [citation needed] and are also used in other areas of biochemistry. The Hill equation can be used to describe dose-response relationships, for example ion channel open-probability (P-open) vs. ligand concentration. [15]
An example of a Lineweaver–Burk plot of 1/v against 1/a. In biochemistry, the Lineweaver–Burk plot (or double reciprocal plot) is a graphical representation of the Michaelis–Menten equation of enzyme kinetics, described by Hans Lineweaver and Dean Burk in 1934. [1]
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