Title : Loss of conformational stability in calmodulin upon methionine oxidation.

Pub. Date : 1998 Mar

PMID : 9512014






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Loss of conformational stability in calmodulin upon methionine oxidation. Methionine CaM5 Triticum aestivum
2 We have used electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD), and fluorescence spectroscopy to investigate the secondary and tertiary structural consequences that result from oxidative modification of methionine residues in wheat germ calmodulin (CaM), and prevent activation of the plasma membrane Ca-ATPase. Methionine CaM5 Triticum aestivum
3 We have used electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD), and fluorescence spectroscopy to investigate the secondary and tertiary structural consequences that result from oxidative modification of methionine residues in wheat germ calmodulin (CaM), and prevent activation of the plasma membrane Ca-ATPase. Methionine CaM5 Triticum aestivum
4 Using ESI-MS, we have measured rates of modification and molecular mass distributions of oxidatively modified CaM species (CaMox) resulting from exposure to H2O2. camox CaM5 Triticum aestivum
5 Using ESI-MS, we have measured rates of modification and molecular mass distributions of oxidatively modified CaM species (CaMox) resulting from exposure to H2O2. Hydrogen Peroxide CaM5 Triticum aestivum
6 Because the opposing globular domains remain spatially distant in both native and oxidatively modified CaM, the oxidative modification of methionines in the carboxyl-terminal domain are suggested to modify the conformation of the amino-terminal domain through alterations in the structural features involving the interdomain central helix. Methionine CaM5 Triticum aestivum