P-39 CaM and OMP interaction monitored by the QCM-D sensor
Presenter Status
Department of Engineering and Computer Science
Location
Buller Hallway
Start Date
1-11-2013 1:30 PM
End Date
1-11-2013 3:00 PM
Presentation Abstract
Olfactory marker protein (OMP, 19kDa) is a ubiquitous, cytoplasmic protein found in mature olfactory receptor neurons of all vertebrates. Calmodulin (CaM, 17kDa) is a ubiquitous Ca2+ sensor and has a wide range of binding partners in the olfactory sensory cascade. Although CaM has been studied extensively, however, OMP’s role in olfactory neuron has been enigmatic. We tested CaM (or OMP) and various peptides in the olfactory cascade to identify its roles using the QCM-D sensor and NMR. We proved that OMP and CaM shares the same binding motif to many proteins in the olfactory sensory transduction. Moreover, OMP and CaM were observed to bind to one another in the pull-down assay and QCM-D sensor. The results suggest that OMP is deeply related to regulating CaM’s function in the olfactory sensory transduction.
P-39 CaM and OMP interaction monitored by the QCM-D sensor
Buller Hallway
Olfactory marker protein (OMP, 19kDa) is a ubiquitous, cytoplasmic protein found in mature olfactory receptor neurons of all vertebrates. Calmodulin (CaM, 17kDa) is a ubiquitous Ca2+ sensor and has a wide range of binding partners in the olfactory sensory cascade. Although CaM has been studied extensively, however, OMP’s role in olfactory neuron has been enigmatic. We tested CaM (or OMP) and various peptides in the olfactory cascade to identify its roles using the QCM-D sensor and NMR. We proved that OMP and CaM shares the same binding motif to many proteins in the olfactory sensory transduction. Moreover, OMP and CaM were observed to bind to one another in the pull-down assay and QCM-D sensor. The results suggest that OMP is deeply related to regulating CaM’s function in the olfactory sensory transduction.