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
Hauptverfasser: Brzeska, Hanna, Venyaminov, Sergey Vu, Grabarek, Zenon, Drabikowski, Witold
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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(83)80141-0