Calcium binding to the low affinity sites in troponin C induces conformational changes in the high affinity domain. A possible route of information transfer in activation of muscle contraction.
Open Access
- 1 January 1986
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 261 (2) , 608-613
- https://doi.org/10.1016/s0021-9258(17)36135-5
Abstract
No abstract availableThis publication has 42 references indexed in Scilit:
- Fluorescence lifetime and acrylamide quenching studies of the interactions between troponin subunitsBiochemistry, 1984
- Calcium-dependent inhibitory region of troponin: a proton nuclear magnetic resonance study on the interaction between troponin C and the synthetic peptide N.alpha.-acetyl[FPhe106]TnI-(104-115) amideBiochemistry, 1983
- Interaction between troponin I and troponin CFEBS Letters, 1982
- Fluorescence energy transfer studies of skeletal troponin C proximity between methionine-25 and cysteine-98Biochemistry, 1982
- Comparison of the Mg2+ and Ca2+ Binding Properties of Troponin Complexes P1‐TI2C and TI2CEuropean Journal of Biochemistry, 1980
- SYNTHETIC STUDIES ON TROPONIN I ACTIVE SITE. PREPARATION OF A PENTADECAPEPTIDE WITH INHIBITORY ACTIVITY TOWARD ACTOMYOSIN ADENOSINE TRIPHOSPHATASEChemistry Letters, 1980
- Protein-protein interaction sites in the calcium modulated skeletal muscle troponin complexJournal of Inorganic Biochemistry, 1980
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Troponin, tripomyosin, and actin interactions in the Ca2+ion regulation of muscle contractionBiochemistry, 1974
- Ca++ induced conformational changes in the Ca++ binding component of troponinBiochemical and Biophysical Research Communications, 1972