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- W1602749230 abstract "Conformations of the regulatory domain of cardiac troponin C (cNTnC) were studied by means of residual dipolar couplings measured from samples dissolved in dilute liquid crystals. Changes in the main chain HN residual dipolar couplings revealed a conformational change in cNTnC due to the complexation with the second binding region (amino acids 148-163) of cardiac troponin I (cTnI). Formation of the complex is accompanied with a molecular realignment in the liquid crystal. The residual dipolar couplings measured for apo-cNTnC and the complex with TnI were in agreement with the values computed from the corresponding closed and open solution structures, whereas for the calcium-loaded conformation the correlation and quality factor were only modest. Ca2+-cNTnC may be subject to conformational exchange. The data support the model that cardiac troponin C functions as a calcium-dependent open-closed switch, such as the skeletal troponin C." @default.
- W1602749230 created "2016-06-24" @default.
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- W1602749230 date "2000-11-01" @default.
- W1602749230 modified "2023-10-17" @default.
- W1602749230 title "Conformations of the regulatory domain of cardiac troponin C examined by residual dipolar couplings" @default.
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- W1602749230 doi "https://doi.org/10.1046/j.1432-1327.2000.01763.x" @default.
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