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The Q 10 coefficient represents the degree of temperature dependence a muscle exhibits as measured by contraction rates. [2] A Q 10 of 1.0 indicates thermal independence of a muscle whereas an increasing Q 10 value indicates increasing thermal dependence. Values less than 1.0 indicate a negative or inverse thermal dependence, i.e., a decrease ...
in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA. Conservation of enzyme requires that [28] = where is now the total enzyme concentration. After combining the two expressions some straightforward algebra leads to the following expression for the concentration ...
For a given enzyme concentration and for relatively low substrate concentrations, the reaction rate increases linearly with substrate concentration; the enzyme molecules are largely free to catalyse the reaction, and increasing substrate concentration means an increasing rate at which the enzyme and substrate molecules encounter one another.
The rate of a reaction is the concentration of substrate disappearing (or product produced) per unit time (mol L −1 s −1).. The % purity is 100% × (specific activity of enzyme sample / specific activity of pure enzyme).
In physical chemistry, the Arrhenius equation is a formula for the temperature dependence of reaction rates.The equation was proposed by Svante Arrhenius in 1889, based on the work of Dutch chemist Jacobus Henricus van 't Hoff who had noted in 1884 that the Van 't Hoff equation for the temperature dependence of equilibrium constants suggests such a formula for the rates of both forward and ...
Data from reaction progress kinetics experiments are also often presented via a rate (v) vs. substrate concentration ([S]) plot. This requires obtaining and combining both the [S] vs. t and the v vs. t plots described above (note that one may be obtained from the other by simple differentiation or integration.)
Soon thereafter, Linus Pauling proposed that the powerful catalytic action of enzymes could be explained by specific tight binding to the transition state species [26] Because reaction rate is proportional to the fraction of the reactant in the transition state complex, the enzyme was proposed to increase the concentration of the reactive species.
The relative activity of a species i, denoted a i, is defined [4] [5] as: = where μ i is the (molar) chemical potential of the species i under the conditions of interest, μ o i is the (molar) chemical potential of that species under some defined set of standard conditions, R is the gas constant, T is the thermodynamic temperature and e is the exponential constant.