Role of the structural domain of troponin C in muscle regulation: NMR studies of Ca2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I.

@article{Mercier2000RoleOT,
  title={Role of the structural domain of troponin C in muscle regulation: NMR studies of Ca2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I.},
  author={Pascal Mercier and Monica X. Li and Brian D. Sykes},
  journal={Biochemistry},
  year={2000},
  volume={39 11},
  pages={2902-11}
}
The interaction between the calcium binding and inhibitory components of troponin is central to the regulation of muscle contraction. In this work, two-dimensional heteronuclear single-quantum coherence nuclear magnetic resonance (2D-¿1H,15N¿-HSQC NMR) spectroscopy was used to determine the stoichiometry, affinity, and mechanisms for binding of Ca2+ and two synthetic TnI peptides [TnI1-40 (or Rp40) and TnI96-115] to the isolated C-domain of skeletal troponin C (CTnC). The Ca2+ titration… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 12 extracted citations

Regulating the contraction of insect flight muscle

Journal of Muscle Research and Cell Motility • 2011
View 2 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…