A thermodynamic and electron paramagnetic resonance study of structural changes in calmodulin induced by aluminum binding.

[1]  A. Haug,et al.  Aluminum interaction with calmodulin. Evidence for altered structure and function from optical and enzymatic studies. , 1983, Biochimica et biophysica acta.

[2]  J. Gergely,et al.  Metal-binding properties of calmodulin. , 1982, European journal of biochemistry.

[3]  J. Gergely,et al.  Binding of lanthanide ions to troponin C. , 1981, Biochemistry.

[4]  D. Puett,et al.  SPIN LABELED CALMODULIN: A NEW PROBE FOR STUDYING Ca2+ AND MACROMOLECULAR INTERACTIONS * , 1980, Annals of the New York Academy of Sciences.

[5]  L. Packer,et al.  An imidoester spin probe of membrane protein interactions: application to cytochrome c. , 1980, Archives of biochemistry and biophysics.

[6]  J. Demaille,et al.  Terbium as luminescent probe of calmodulin calcium‐binding sites , 1980, FEBS letters.

[7]  J. Potter,et al.  Thermodynamics of Ca2+ binding to troponin-C. , 1977, The Journal of biological chemistry.

[8]  J. H. Wang,et al.  Calmodulin and its role in the second-messenger system. , 1979, Current topics in cellular regulation.

[9]  W. Kauzmann.  Some factors in the interpretation of protein denaturation. , 1959, Advances in protein chemistry.