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Calcium and peptide binding to folded and unfolded conformations of cardiac Troponin C. Electrospray ionization and Fourier transform ion cyclotron resonance mass spectrometry
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UNSPECIFIED (2002) Calcium and peptide binding to folded and unfolded conformations of cardiac Troponin C. Electrospray ionization and Fourier transform ion cyclotron resonance mass spectrometry. EUROPEAN JOURNAL OF MASS SPECTROMETRY, 8 (6). pp. 471-481. doi:10.1255/ejms.523 ISSN 1469-0667.
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Official URL: http://dx.doi.org/10.1255/ejms.523
Abstract
The binding of Ca2+ and of a peptide (N-TnI) to human cardiac troponin C (TnC) and its isolated N- and C-terminal domains has been characterized by electrospray ionization Fourier transform ion cyclotron resonance (ESI FT-ICR) mass spectrometry. The peptide N-TnI corresponds to residues 1-29 of the cardiac-specific N-terminal extension of human cardiac troponin I (TnI). The binding of Ca2+ to intact TnC in the absence of the peptide was found to take a bimodal form with preferred stoichiometries of 1 : 1 TnC : Ca2+ and 1 : 3 TnC : Ca2+. It is concluded that TnC existed in two conformational isomers that had different binding affinities for Ca2+: the binding of 3 Ca2+ was characteristic of a folded conformation (TnC(A)) and the binding of 1 Ca2+ was characteristic of a partially unfolded conformation (TnC(B)). Both of these conformations contributed to the 8+ (and other) charge states of TnC, and were distinguished on the basis of their different Ca2+-binding affinities and not on the basis of the charge state. In the presence of the peptide, a complex with 1 : 1 : 1 TnC : peptide : Ca2+ stoichiometry was formed.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QC Physics | ||||
| Journal or Publication Title: | EUROPEAN JOURNAL OF MASS SPECTROMETRY | ||||
| Publisher: | IM PUBLICATIONS | ||||
| ISSN: | 1469-0667 | ||||
| Official Date: | 2002 | ||||
| Dates: |
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| Volume: | 8 | ||||
| Number: | 6 | ||||
| Number of Pages: | 11 | ||||
| Page Range: | pp. 471-481 | ||||
| DOI: | 10.1255/ejms.523 | ||||
| Publication Status: | Published |
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