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- W2078443597 abstract "Troponin is the thin filament protein that confers tight, Ca2+-dependent control over muscle contraction. The mechanism of this regulation was investigated by detailed mapping of the dynamic properties of cardiac troponin, using amide hydrogen exchange-mass spectrometry, in the presence of either saturation or non-saturation of the regulatory Ca2+ binding site in the NH2-domain of subunit TnC. Troponin was found to be highly dynamic, with 60% of amides exchanging H for D within seconds of exposure to D2O. In contrast, portions of the TnT-TnI coiled-coil exhibited high protection from exchange, more than six hours, identifying the most stable portion of the trimeric troponin complex. Regulatory site Ca2+ binding altered dynamic properties (i.e., H/D exchange protection) locally, near the binding site and in the TnI switch helix that attaches to the Ca2+-saturated TnC NH2-domain. More notably, Ca2+ also altered the dynamic properties of other parts of troponin: the TnI inhibitory peptide region that binds to actin, the TnT-TnI coiled-coil, and the TnC COOH-domain that contains the regulatory Ca2+ sites in many invertebrate as opposed to vertebrate troponins. Mapping of these affected regions onto troponin's highly extended structure indicates contacts important in conformational change: in the low Ca2+ state the TnI region that effects inhibition bends back and interacts with the end of the TnT-TnI coiled-coil, as previously suggested by intermediate resolution X-ray data of skeletal muscle troponin. Thus, troponin-mediated Ca2+ sensitive regulation of muscle contraction consists of Ca2+-triggered switching between alternative sets of intra-troponin interactions." @default.
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- W2078443597 date "2010-01-01" @default.
- W2078443597 modified "2023-09-26" @default.
- W2078443597 title "Troponin Regulatory Function and Dynamics Revealed by H/D Exchange-Mass Spectrometry" @default.
- W2078443597 doi "https://doi.org/10.1016/j.bpj.2009.12.2239" @default.
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