Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy
Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy
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DOI：
10.1021/ja046578g
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发表时间：
2004-09-22
影响因子：
15
通讯作者：
Emsley, L
中科院分区：
文献类型：
--
作者：
Giraud, N;Böckmann, A;Emsley, L
使用多维高分辨率固态核磁共振方法测量了蛋白质Crh的微晶二聚体形式的位点特异性氮-15纵向弛豫率。测量的速率用于提供固体状态下蛋白质的特定位点内部迁移率的定性描述。
Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a qualitative description of the site-specific internal mobility of the protein present in the solid state.