Ca2+ and Mg2+ dependent conformations of troponin C as determined by 1H and 19F nuclear magnetic resonance.

[1]  G. Strichartz,et al.  On the voltage-dependent action of tetrodotoxin. , 1977, Biophysical journal.

[2]  J. Potter,et al.  Effect of Ca2+ binding on troponin C. Changes in spin label mobility, extrinsic fluorescence, and sulfhydryl reactivity. , 1976, The Journal of biological chemistry.

[3]  C. Dobson,et al.  Conformational mobility within the structure of muscular parvalbumins. An NMR study of the aromatic resonances of phenylalanine residues , 1976, FEBS letters.

[4]  G. Lowe,et al.  Co-operative ionisation of aspartic-acid-158 and histidine-159 in papain. Evidence from 19F nuclear-magnetic-resonance and fluorescence spectroscopy. , 1976, European journal of biochemistry.

[5]  B. Sykes,et al.  Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: the influence of zinc on protein structure and a conformational change induced by phosphate binding. , 1976, Biochemistry.

[6]  J. Thornton,et al.  Proton magnetic resonance study of troponin‐C , 1976, FEBS letters.

[7]  T. L. Miller,et al.  Calcium binding sites of rabbit troponin and carp parvalbumin , 1975, FEBS letters.

[8]  C. D. Barry,et al.  The predicted structure of the calcium-binding component of troponin. , 1975, Biochimica et biophysica acta.

[9]  B. Sykes,et al.  Complete tyrosine assignments in the high field 1H nuclear magnetic resonance spectrum of the bovine pancreatic trypsin inhibitor. , 1975, Biochemistry.

[10]  K. Hiromi,et al.  Studies on the subsite structure of amylases. II. Difference-spectrophotometric studies on the interaction of maltotriose with liquefying alpha-amylase from Bacillus subtilis. , 1975, Journal of biochemistry.

[11]  C. Kay,et al.  The influence of calcium on the spectral properties of the nitrotyrosyl chromophore in troponin C , 1975, FEBS letters.

[12]  J. Bode,et al.  19F nuclear magnetic resonance studies of structure and function relationships in trifluoroacetonylated rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. , 1975, Biochemistry.

[13]  R. Kretsinger,et al.  Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme. , 1975, Science.

[14]  A. Mclachlan,et al.  Structural homology of myosin alkali light chains, troponin C and carp calcium binding protein , 1974, Nature.

[15]  S. Lehrer,et al.  Fluorescence and conformational changes caused by proton binding to troponin C. , 1974, Biochemical and biophysical research communications.

[16]  C. Maury,et al.  Conformational studies on muscular parvalbumins. II. Nuclear magnetic resonance analysis. , 1974, Biochimie.

[17]  J. Dadok,et al.  Correlation NNW spectroscopy , 1974 .

[18]  S. Perry,et al.  The interaction of the calcium-binding protein (troponin C) with bivalent cations and the inhibitory protein (troponin I). , 1974, The Biochemical journal.

[19]  J. Demaille,et al.  Evolutionary Aspects of the Structure of Muscular Parvalbumins , 1973 .

[20]  J. H. Collins,et al.  The amino acid sequence of rabbit skeletal muscle troponin C: Gene replication and homology with calcium ‐binding proteins from carp and hake muscle , 1973, FEBS letters.

[21]  R. Kretsinger,et al.  Carp muscle calcium-binding protein. II. Structure determination and general description. , 1973, The Journal of biological chemistry.

[22]  C. Kay,et al.  Hydrodynamic and optical properties of troponin A. Demonstration of a conformational change upon binding calcium ion. , 1972, Biochemistry.

[23]  Y. Kawasaki,et al.  Ca ++ induced conformational changes in the Ca ++ binding component of troponin. , 1972, Biochemical and biophysical research communications.

[24]  M. Raftery,et al.  A study of cooperative interactions in hemoglobin using fluorine nuclear magnetic resonance. , 1972, Biochemistry.

[25]  J. Gergely,et al.  Reconstitution of troponin activity from three protein components. , 1971, The Journal of biological chemistry.

[26]  M. Morrison,et al.  Catalysis of iodination by lactoperoxidase. , 1970, Biochemistry.

[27]  R. Cowgill Fluorescence and the structure of proteins. XII. Pancreatic trypsin inhibitor. , 1967, Biochimica et biophysica acta.

[28]  D. D. Perrin,et al.  Computer calculation of equilibrium concentrations in mixtures of metal ions and complexing species. , 1967, Talanta.

[29]  D. Wallach,et al.  Fluorescence Techniques in the Microdetermination of Metals in Biological Materials. Utility of 2, 4-Bis-[N,N´-di-(carboxymethyl)aminomethyl] Fluorescein in the Fluorometric Estimation of Al+3, Alkaline Earths, Co+2, Cu+2, Ni+2, and Zn+2 in Micromolar Concentrations. , 1963 .

[30]  Oliver H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.

[31]  S. Ebashi,et al.  Troponin and its components. , 1971, Journal of biochemistry.

[32]  S. Ebashi,et al.  Calcium ion and muscle contraction. , 1968, Progress in biophysics and molecular biology.

[33]  Richard R. Ernst,et al.  Sensitivity Enhancement in Magnetic Resonance , 1966 .