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Direct 19F NMR observation of the conformational selection of optically active rotamers of the antifolate compound fluoronitropyrimethamine bound to the enzyme dihydrofolate reductase

机译：直接19F NMR观察结合到二氢叶酸还原酶上的抗叶酸化合物氟硝基嘧啶的旋光性旋转异构体的构象选择

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Tendler Saul J.B.; Griffin Roger J.; Birdsall Berry; Stevens Malcolm F.G.; Roberts Gordon C.K.; Feeney James;
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年度 1988
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1. Direct 19F NMR observation of the conformational selection of optically active rotamers of the antifolate compound fluoronitropyrimethamine bound to the enzyme dihydrofolate reductase [J] . Birdsall Berry, Feeney James, Griffin Roger J., FEBS Letters . 1988,第1a2期

机译：直接19F NMR观察结合到二氢叶酸还原酶上的抗叶酸化合物氟硝基嘧啶的旋光性旋转异构体的构象选择
2. Direct 19F NMR observation of the conformational selection of optically active rotamers of the antifolate compound fluoronitropyrimethamine bound to the enzyme dihydrofolate reductase [J] . Birdsall Berry, Feeney James, Griffin Roger J., FEBS Letters . 1988,第1a2期

机译：直接19F NMR观察结合到二氢叶酸还原酶上的抗叶酸化合物氟硝基嘧啶的旋光性旋转异构体的构象选择
3. Crystal Structures of Candida albicans Dihydrofolate Reductase Bound to Propargyl- Linked Antifolates Reveal the Flexibility of Active Site Loop Residues Critical for Ligand Potency and Selectivity [J] . Janet L. Paulsen, Stephen D. Bendel, Amy C. Anderson Chemical biology and drug design . 2011,第4期

机译：白色念珠菌二氢叶酸还原酶绑定到炔丙基连接的抗叶酸的晶体结构揭示了活性位点环残基的灵活性，这对配体的效能和选择性至关重要
4. Crystal structures of Candida albicans dihydrofolate reductase bound to propargyl-linked antifolates reveal the flexibility of active site loop residues critical for ligand potency and selectivity [O] . Janet L. Paulsen, Stephen D. Bendel, Amy C. Anderson -1

机译：念珠菌蛋白质的晶体结构二氢酚酸还原酶与炔丙基连接的抗雾化物结合揭示了活性位点回物残留物的柔韧性对于配体效力和选择性至关重要
5. Crystal Structures of Candida albicans Dihydrofolate Reductase Bound to Propargyl-Linked Antifolates Reveal the Flexibility of Active Site Loop Residues Critical for Ligand Potency and Selectivity [O] . Janet L. Paulsen, Stephen D. Bendel, Amy C. Anderson 2011

机译：念珠菌蛋白质的晶体结构二氢酚酸还原酶与炔丙基连接的抗雾化物结合揭示了活性位点回物残留物的柔韧性，对于配体效力和选择性至关重要

Direct 19F NMR observation of the conformational selection of optically active rotamers of the antifolate compound fluoronitropyrimethamine bound to the enzyme dihydrofolate reductase

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