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A synthetic peptide mimics troponin I function in the calcium‐dependent regulation of muscle contraction
Author(s) -
Van Eyk Jennifer E.,
Strauss John D.,
Hodges Robert S.,
Rüegg J.Casper
Publication year - 1993
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(93)81344-y
Subject(s) - troponin , actin , troponin c , troponin i , troponin complex , peptide , biophysics , chemistry , muscle contraction , troponin t , calcium , contraction (grammar) , muscle relaxation , tropomyosin , biochemistry , medicine , biology , organic chemistry , myocardial infarction
A new technique for treating skinned cardiac muscle fibers has been developed in which troponin I is extracted, giving rise to unregulated fibers. The effect of the 12‐residue troponin I peptide on these fibers indicates that this region of troponin I is solely responsible for muscle relaxation (inhibition of force). Furthermore, troponin I peptide‐troponin C reconstituted fibers are stable through several contraction‐relaxation cycles indicating the peptide can switch binding sites between actin and troponin C. The troponin I peptide can substitute for the native protein as part of the calcium‐sensitive molecular switch that controls muscle regulation.