The structure of calmodulin and its specific interaction with several proteins will be examined, using a range of physical techniques. The molecular dynamics of calmodulin will be studied by measurements of the time decay of fluorescence anisotropy, as well as static anisotropy measurements, employing specifically located fluorescent probes. Particular attention will be paid to the effects of temperature and complex formation. The interaction of calmodulin with polypeptide hormones, troponin I, and myosin light chain kinase will be studied in detail. Radiationless energy transfer will be employed to investigate the spatial organization of complexes of calmodulin with other proteins.
| Bucci, E; Steiner, R F (1990) Perturbation of molecular species distribution in steady states supported by a flow of energy. Models analogous to Ca2(+)-dependent ATPase and phosphorylase b. Biophys Chem 37:61-71 |
| Garone, L; Steiner, R F (1990) The interaction of calmodulin with the C-terminal M5 peptide of myosin light chain kinase. Arch Biochem Biophys 276:12-8 |
| Lan, J; Albaugh, S; Steiner, R F (1989) Interactions of troponin I and its inhibitory fragment (residues 104-115) with troponin C and calmodulin. Biochemistry 28:7380-5 |
| Eames, T C; Pollack, R M; Steiner, R F (1989) Orientation, accessibility, and mobility of equilenin bound to the active site of steroid isomerase. Biochemistry 28:6269-75 |
