Letter to the Editor: 1H, 15N and 13C resonance assignments of yeast Saccharomyces cerevisiaecalmodulin in the Ca2+-free state
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Calmodulin (CaM) is a small Ca2+-binding protein, which has been found in all of eucaryotic cells examined. CaMs isolated from various species have highly conserved amino acid sequence (more than 90% identical), and show the same biological functions. CaM isolated from the baker's yeast (Saccharomyces cerevisiae) (yCaM), however, shares only 60% identity in the amino acid sequence with CaM from vertebrate, and shows quite distinct conformational and biochemical properties compared with those of CaM from other species. The conformational details of yCaM, however, have not been revealed yet. We achieved the chemical shift assignments of yCaM (146 amino acids) in the apo-state using uniformly 15N- and 13C-labeled protein. Consequently, the resonances of 95% atoms in the backbone amides were successfully assigned.
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- Letter to the Editor: 1H, 15N and 13C resonance assignments of yeast Saccharomyces cerevisiaecalmodulin in the Ca2+-free state
Journal of Biomolecular NMR
Volume 23, Issue 4 , pp 323-324
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- chemical shift assignments
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- Author Affiliations
- 1. Divisions of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, 060-0810, Japan
- 2. High Resolution NMR Laboratory, Graduate School of Science, Hokkaido University, Sapporo, 060-0810, Japan
- 3. Chemistry, Graduate School of Science, Hokkaido University, Sapporo, 060-0810, Japan