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
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container_title FEBS letters
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creator Brzeska, Hanna
Venyaminov, Sergey Vu
Grabarek, Zenon
Drabikowski, Witold
description 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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subjects Animals
brain
C.D
calcium
Calcium - pharmacology
Calcium-Binding Proteins - metabolism
calmodulin
Calmodulin - metabolism
Cattle
Circular Dichroism
Drug Stability
Hot Temperature
magnesium
Magnesium - pharmacology
Muscle Proteins - metabolism
Peptide Fragments - metabolism
Protein Conformation - drug effects
Rabbits
secondary structure
skeletal muscle
thermal stability
Troponin - metabolism
Troponin C
Trypsin
title Comparative studies on thermostability of calmodulin, skeletal muscle troponin C and their tryptic fragments
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