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Interaction between troponin I and troponin C
Author(s) -
Dalgarno D.C.,
Grand R.J.A.,
Levine B.A.,
Moir A.J.G.,
Scott G.M.M.,
Perry S.V.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81303-3
Subject(s) - troponin c , troponin i , troponin complex , troponin , chemistry , peptide , paramagnetism , troponin t , biophysics , nuclear magnetic resonance , biochemistry , cardiology , medicine , physics , biology , myocardial infarction , quantum mechanics
The spatial proximity on the surface of troponin C for sites specific for peptides CN4 (res. 96–116) and CN5 (res. 1–21) of troponin I has been demonstrated by proton magnetic resonance spectroscopy. The broadened signals from each peptide are at similar radial distances from the paramagnetic spin label bound to Cys 98 of troponin C. A U‐shaped disposition of peptide CN5 about Cys 98 is indicated, the interaction being modulated by calcium binding to the low affinity Ca 2+ domains of troponin C. Paramagnetic broadening of signals from peptide CN4 was observed on addition of peptide TR2 (res. 88–159) from spin‐labelled troponin C, a region that contains the higher affinity Ca 2+ domains.