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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 ...
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:
One manifestation of this is enzymes or receptors that have multiple binding sites where the affinity of the binding sites for a ligand is apparently increased, positive cooperativity, or decreased, negative cooperativity, upon the binding of a ligand to a binding site. For example, when an oxygen atom binds to one of hemoglobin's four binding ...
At the regulatory site, the binding of a ligand may elicit amplified or inhibited protein function. [ 4 ] [ 22 ] The binding of a ligand to an allosteric site of a multimeric enzyme often induces positive cooperativity, that is the binding of one substrate induces a favorable conformation change and increases the enzyme's likelihood to bind to ...
A protein–ligand complex is a complex of a protein bound with a ligand [2] that is formed following molecular recognition between proteins that interact with each other or with other molecules. Formation of a protein-ligand complex is based on molecular recognition between biological macromolecules and ligands, where ligand means any molecule ...
Homology model of the DHRS7B protein created with Swiss-model and rendered with PyMOL. Homology modeling, also known as comparative modeling of protein, refers to constructing an atomic-resolution model of the "target" protein from its amino acid sequence and an experimental three-dimensional structure of a related homologous protein (the "template").
It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: R + L ⇌ RL. The reaction is characterized by the on-rate constant k on and the off-rate constant k off, which have units of M −1 s −1 and s −1, respectively. In equilibrium, the forward binding transition R + L → ...
In bioinformatics, LIGPLOT is a computer program that generates schematic 2-D representations of protein-ligand complexes from standard Protein Data Bank file input. [1] The LIGPLOT is used to generate images for the PDBsum resource that summarises molecular structure.