Comparative studies on thermostability of calmodulin, skeletal muscle troponin C and their tryptic fragments
To obtain additional information about the effect of Ca super(2+) and Mg super(2+) on the secondary structure of Ca super(2+)-binding proteins, the authors studied thermostability of skeletal muscle troponin C and calmodulin using circular dichroism technique and the influence of Ca super(2+)-and Mg...
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Veröffentlicht in: | FEBS letters 1983-03, Vol.153 (1), p.169-173 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | To obtain additional information about the effect of Ca super(2+) and Mg super(2+) on the secondary structure of Ca super(2+)-binding proteins, the authors studied thermostability of skeletal muscle troponin C and calmodulin using circular dichroism technique and the influence of Ca super(2+)-and Mg super(2+)-binding on thermal unfolding. Tryptic fragments of both calcium-binding proteins were used to localise the structural changes caused by temperature changes in the particular parts of both molecules. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(83)80141-0 |