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The Hill equation reflects the occupancy of macromolecules: the fraction that is saturated or bound by the ligand. [1] [2] [nb 1] This equation is formally equivalent to the Langmuir isotherm. [3] Conversely, the Hill equation proper reflects the cellular or tissue response to the ligand: the physiological output of the system, such as muscle ...
Hill's equation is an important example in the understanding of periodic differential equations. Depending on the exact shape of (), solutions may stay bounded for all time, or the amplitude of the oscillations in solutions may grow exponentially. [3] The precise form of the solutions to Hill's equation is described by Floquet theory. Solutions ...
The Hill equation can be used to describe dose–response relationships, for example ion channel-open-probability vs. ligand concentration. [9] Dose is usually in milligrams, micrograms, or grams per kilogram of body-weight for oral exposures or milligrams per cubic meter of ambient air for inhalation exposures. Other dose units include moles ...
The EC 50 relates to the Hill equation, which is a function of the agonist concentration, [A]: = [] [] + [3] where E is the observed response or effect above baseline, and n, the Hill coefficient reflects the slope of the curve. [7]
The first description of cooperative binding to a multi-site protein was developed by A.V. Hill. [4] Drawing on observations of oxygen binding to hemoglobin and the idea that cooperativity arose from the aggregation of hemoglobin molecules, each one binding one oxygen molecule, Hill suggested a phenomenological equation that has since been named after him:
If the enzyme is irreversible the equation turns into the simple Michaelis-Menten equation that is irreversible. When setting the equilibrium constant to infinity, the equation can be seen to revert to the simpler case where the product inhibits the reverse step. A comparison has been made between the MWC and reversible Hill equation. [9]
The Hill equation [40] is often used to describe the degree of cooperativity quantitatively in non-Michaelis–Menten kinetics. The derived Hill coefficient n measures how much the binding of substrate to one active site affects the binding of substrate to the other active sites.
Although Hill's equation looks very much like the van der Waals equation, the former has units of energy dissipation, while the latter has units of energy. Hill's equation demonstrates that the relationship between F and v is hyperbolic. Therefore, the higher the load applied to the muscle, the lower the contraction velocity.