Simple method to identify and characterize binding-induced conformational change of surface immobilized proteins using a QCM-D sensor. CaM was used because it is a well-studied molecule for conformation change when binding. To demonstrate the versatile dynamics of binding characteristics, it would be ideal to choose peptides from a series of proteins that work in concert within a single cell. As a model system, peptides were derived from proteins present in a single olfactory sensory neuron. CaM plays a pivotal role in olfactory signal transduction cascade by regulating a number of channels, enzymes and receptors, such as olfactory cyclic nucleotide-gated (CNG) channels, ryanodine receptors (RYRs), plasma membrane calcium-ATPase (PMCA), and 3’, 5’-cluclic nucleotide phosphodiesterase (PDE), plasma membrane sodium-calcium exchanger (NCX), etc.
Citation: Kwon HJ, Dodge BT (2015) QCM-D Monitoring of Binding-Induced Conformational Change of Calmodulin. Biosens J 4:126