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Alternative online IC50 calculator (www.ic50.org) based on Python, NumPy, SciPy and Matplotlib; ELISA IC50/EC50 Online Tool (link seems broken) IC50 to pIC50 calculator; Online tool for analysis of in vitro resistance to antimalarial drugs; IC50-to-Ki converter of an inhibitor and enzyme that obey classic Michaelis-Menten kinetics
Lipophilic efficiency [1] (LiPE), sometimes referred to as ligand-lipophilicity efficiency (LLE) is a parameter used in drug design and drug discovery to evaluate the quality of research compounds, linking potency and lipophilicity in an attempt to estimate druglikeness.
Ligand efficiency is a measurement of the binding energy per atom of a ligand to its binding partner, such as a receptor or enzyme. [1]Ligand efficiency is used in drug discovery research programs to assist in narrowing focus to lead compounds with optimal combinations of physicochemical properties and pharmacological properties.
The parameters of the dose response curve reflect measures of potency (such as EC50, IC50, ED50, etc.) and measures of efficacy (such as tissue, cell or population response). A commonly used dose–response curve is the EC 50 curve, the half maximal effective concentration, where the EC 50 point is defined as the inflection point of the curve.
Biological responses to ligand concentrations typically follow a sigmoidal function. The inflection point at which the increase in response with increasing ligand concentration begins to slow is the EC 50, which can be mathematically determined by derivation of the best-fit line.
Hill equation calculator This page was last edited on 23 January 2025, at 04:36 (UTC). Text is available under the Creative Commons Attribution-ShareAlike 4.0 ...
Inhibitors have IC50 values so I tried to reintegrate it with information already present in the article. I think that including it in the lead paragraph would mislead people into thinking it was a discussion about inhibitors not The IC50 concept Lilypink 19:04, 5 November 2007 (UTC) IC50 is not a pharmacological constant! pA2 is a constant.
Hydrophobicity scales are values that define the relative hydrophobicity or hydrophilicity of amino acid residues. The more positive the value, the more hydrophobic are the amino acids located in that region of the protein.