Research Interests   Membrane biophysics, calcium regulation in muscle, ryanodine receptor calcium channels

Research Description
My current research is focused on understanding the molecular interacttions and structural events that underlie the gating and regulationof the 2.3 million dalton ryanodine receptor (RyR) channel complex in normal and dysfunctional muscle. Calmodulin (CaM) and FKBP12 are two accessory proteins that bind with high affinity at discrete sites on RyR. Fluorescent derivatives of CaM and KFBP12 are emmployed as structural probes of the RyR channels. High-sensiriity, high-throughput fluorescence spectroscopic approaches are used to identify structure-function correlations within RyRs. Ultimately, we hope to contribute to elucidating the basis of altered RyR function in muscle diseases.

Fruen, B.R., Balog, E.M., Schafer, J., Nitu, F.R., Thomas, D.D., and Cornea, R.L. (2005) Direct detection of calmodulin tuning by ryanodine receptor channel targets using a Ca²⁺-sensitive acrylodan-labeled calmodulin. Biochemistry 44, 278-284.

Balog, E.M., Norton, L.E., Bloomquist, R.A, Cornea, R.L., Black, D.J., Louis, C.F., Thomas, D.D., and Fruen, B.R. (2003) Calmodulin oxidation and methionine to glutamine substitutions reveal methionine residues critical for functional interaction with RyR1. J. Biol. Chem. 278, 15615-15621.

Reddy, L.G., Cornea, R.L., Winters, D.L., McKenna, E., and Thomas, D.D. (2003) Defining the molecular components of calcium transport regulation in a reconstituted membrane system. Biochemistry 42, 4585-4592.

Jones, L.R., Cornea, R.L., and Chen, Z. (2002) Close proximity between residue 30 of phospholamban and cysteine 318 of the cardiac Ca²⁺-pump revealed by intermolecular thiol cross-linking. J. Biol. Chem. 277, 28319-28329.