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논문 기본 정보
- 자료유형
- 학술대회자료
- 저자정보
- 발행연도
- 2001.1
- 수록면
- 37 - 37 (1page)
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Cyclic nucleotide-gated (CNG) channels are composed of homo or hetero tetramer of ${\alpha}$ and ${\beta}$ subunits. The a subunits of these channels have a conserved glutamate residue within the pore-forming region. This residue determines the selectivity as well as the affinity for the extracellular divalent cations. Using the high affinity mutant (E363D) of bovine retinal CNG channel in which the Glu was replaced to Asp at position 363, we constructed tandem dimers and investigated the binding symmetry of divalent cation to the site.(omitted)
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