Localization of hydrophobic sites in calmodulin and skeletal muscle troponin C studied using tryptic fragments a simple method of their preparation
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference14 articles.
1. Similarity in Ca2+-induced changes between troponin-C and protein activator of 3′:5′-cyclic nucleotide phosphodiesterase and their tryptic fragments
2. Characterization of tryptic fragments obtained from bovine brain protein modulator of cyclic nucleotide phosphodiesterase.
3. Digestion of troponin C with trypsin in the presence and absence of Ca2+. Identification of cleavage points
4. Proteolytic fragments of troponin C. Localization of high and low affinity Ca2+ binding sites and interactions with troponin I and troponin T
5. Tryptic fragments of calmodulin. Ca2+- and Mg2+-induced conformational changes.
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2. Characterisation of two calmodulin-like proteins from the liver fluke, Fasciola hepatica;Biological Chemistry;2007-06-01
3. Regulatory interaction of sodium channel IQ-motif with calmodulin C-terminal lobe;Biochemical and Biophysical Research Communications;2003-07
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