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• W2012396129 abstract "Abstract By the criterion of their primary structure myosin regulatory light chains belong to the ‘calcium binding protein’ family and are thought to contain domains related to the E-F hand structure found in parvalbumin. However, the presence of deletions and non-conservative substitutions in the regulatory light chains indicates that, of the four domains apparent in their structure, only the first is competent to bind Ca 2+ or other divalent metal ions. Electron paramagnetic resonance studies were performed in an attempt to provide experimental verification of this hypothesis. The approach is based on the finding that the paramagnetic Mn 2+ ion substitutes for Ca 2+ at the divalent metal ion site and that different regulatory light-chain isotypes contain cysteine residues in different domains which may be spin-labelled with a nitroxide derivative. The electron spin interaction between these two paramagnetic centres is a function of the distance of their separation. Clam ( Mercenaria mercenaria ) regulatory light chain contains a single cysteine residue located near the first domain and, when spin-labelled, the intensity of the nitroxide signal is reduced by 25% on binding one mole of Mn 2+ . Rabbit skeletal regulatory light chain contains two cysteine residues located in the third and fourth domains and no ( 2+ binds to spin-labelled derivatives. Qualitatively, these results suggest that domain 1 is the most likely candidate for the Mn 2+ binding site. A more quantitative evaluation using the Leigh (1970) theory for the dipolar coupling between rigid-lattice electron spins and various models for the regulatory light chain tertiary structure, including that predicted by Kretsinger & Barry (1975) for the possibly isologous troponin C structure, substantiates this conclusion." @default.
• W2012396129 created "2016-06-24" @default.
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• W2012396129 date "1980-07-01" @default.
• W2012396129 modified "2023-09-23" @default.
• W2012396129 title "Identification of the divalent metal ion binding domain of myosin regulatory light chains using spin-labelling techniques" @default.
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• W2012396129 doi "https://doi.org/10.1016/0022-2836(80)90392-7" @default.
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