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Example Bjerrum plot: Change in carbonate system of seawater from ocean acidification.. A Bjerrum plot (named after Niels Bjerrum), sometimes also known as a Sillén diagram (after Lars Gunnar Sillén), or a Hägg diagram (after Gunnar Hägg) [1] is a graph of the concentrations of the different species of a polyprotic acid in a solution, as a function of pH, [2] when the solution is at ...
The plot is occasionally attributed to Augustinsson [5] and referred to the Woolf–Augustinsson–Hofstee plot [6] [7] [8] or simply the Augustinsson plot. [9] However, although Haldane, Woolf or Eadie were not explicitly cited when Augustinsson introduced the versus / equation, both the work of Haldane [10] and of Eadie [3] are cited at other places of his work and are listed in his ...
In graph theory, the degree of a vertex is its number of connections. In a chemical graph, the maximum degree of an atom is its valence, and the maximum number of bonds a chemical element can make. For example, carbon's valence is 4. In a chemical graph, an atom is saturated if it reaches its valence.
Pourbaix diagram of iron. [1] The Y axis corresponds to voltage potential. In electrochemistry, and more generally in solution chemistry, a Pourbaix diagram, also known as a potential/pH diagram, E H –pH diagram or a pE/pH diagram, is a plot of possible thermodynamically stable phases (i.e., at chemical equilibrium) of an aqueous electrochemical system.
The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...
Positively cooperative binding: Once one ligand molecule is bound to the enzyme, its affinity for other ligand molecules increases. For example, the Hill coefficient of oxygen binding to haemoglobin (an example of positive cooperativity) falls within the range of 1.7–3.2.
The Lineweaver–Burk plot derives from a transformation of the Michaelis–Menten equation, = + in which the rate is a function of the substrate concentration and two parameters , the limiting rate, and , the Michaelis constant.
The enzyme is integrated into thylakoid membrane; the CF 1-part sticks into stroma, where dark reactions of photosynthesis (also called the light-independent reactions or the Calvin cycle) and ATP synthesis take place. The overall structure and the catalytic mechanism of the chloroplast ATP synthase are almost the same as those of the bacterial ...