Utility of kinetic capillary electrophoresis-mass spectrometry to study protein dynamics and affinity interactions.

摘要

Conformational changes of proteins and their affinity noncovalent interactions with other molecules play a key role in facilitating and regulating biological functions of living systems. Protein dynamics and affinity interactions are also pivotal to bio-catalysis and in de novo protein design with unique catalytic properties. Measuring rate and equilibrium constants are crucial for the understanding of drug actions, as the dissociation rate of drug-protein complexes may be a limiting step for drug elimination and tissue distribution.