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Almost every process in biology can be attributed to an interaction between molecules. With the thousands of
individual molecules that make up a cell, researchers are challenged with determining which types of molecules
interact with each other and figuring out the consequences of these interactions.
Scientists use K
d
to determine or "rank-order" binding reactions that may o en translate into biological function or
uncover the relevance of the targets being examined. The more researchers know about these interactions, the more
they understand the biological systems in which they work with their intricate network of molecular pathways that
control various cellular processes.
Precisely characterizing biomolecular interactions in a biological system is an important cornerstone in basic research.
In applied science, measuring the binding affinity of interactions is a prerequisite for the development of new products,
such as drugs, enzymes or biomarkers. Measuring binding affinity has many applications, including identifying and
screening small and/or large molecules, monitoring the regulation of cellular pathways, screening compound and
drug candidates, testing structure-function relationships, and optimizing the development of assays that examine the
interaction of two molecules.
Why measure
binding affinity?
