Binding assays can be used to either directly detect binding of a ligand to the target or indirectly detect binding through competitive displacement of a probe.
These regions become structured upon binding of a ligand.
A series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell.
The charge conduction properties of DNA can be harnessed for monitoring the binding of a ligand to its receptor.
A series of molecular signals initiated by the binding of a ligand to the receptor Fas on the surface of the cell, and ending with regulation of a downstream cellular process, e.g. transcription.
The binding enthalpy as deduced from isothermal titration calorimetry (ITC) is usually interpreted assuming single-step binding of a ligand to one conformation of the target protein.
In essence, binding of a ligand at an allosteric site affects the function at a distant site exploiting protein flexibility and reshaping protein energy landscape.
The consequences of the binding of a ligand to a receptor are a loss of conformational energy, which is gained by the surroundings.
A series of molecular signals initiated by the binding of a ligand to a beta-type platelet-derived growth factor receptor (PDGFbeta) on the surface of a signal-receiving cell, and ending with regulation of a downstream cellular process, e.g. transcription.
However, binding of a ligand to a receptor is a mutual fitting progress, with conformational changes in both components.
In the parlance of statistical decision theory, the binding of a ligand to a receptor ensemble is a random prospect and realized efficacy is the utility of this prospect.
