PROTEIN C-13 SPIN SYSTEMS BY A SINGLE TWO-DIMENSIONAL NUCLEAR MAGNETIC-RESONANCE EXPERIMENT
PROTEIN C-13 SPIN SYSTEMS BY A SINGLE TWO-DIMENSIONAL NUCLEAR MAGNETIC-RESONANCE EXPERIMENT
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DOI：
10.1126/science.3129784
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发表时间：
1988-05-13
期刊：
影响因子：
56.9
通讯作者：
MARKLEY, JL
中科院分区：
文献类型：
--
作者：
OH, BH;WESTLER, WM;MARKLEY, JL
通过将二维双量子碳-13核磁共振实验应用于均匀富集到26%碳-13的蛋白质，直接键合的碳原子网络凭借其单键自旋耦合被识别，并根据其特定的单量子和双量子化学位移模式按氨基酸类型分类。自旋系统的98个氨基酸残基中的75个蛋白质，氧化Anabaena 7120铁氧还蛋白（分子量11,000），确定了这种方法，这是一个关键步骤，在一个改进的方法分配蛋白质核磁共振谱。丢失的自旋系统主要对应于位于顺磁性铁硫簇附近的残基。
By applying a two-dimensional double-quantum carbon-13 nuclear magnetic resonance experiment to a protein uniformly enriched to 26 percent carbon-13, networks of directly bonded carbon atoms were identified by virtue of their one-bond spin-spin couplings and were classified by amino acid type according to their particular single- and double-quantum chemical shift patterns. Spin systems of 75 of the 98 amino acid residues in a protein, oxidizedAnabaena7120 ferredoxin (molecular weight 11,000), were identified by this approach, which represents a key step in an improved methodology for assigning protein nuclear magnetic resonance spectra. Missing spin systems corresponded primarily to residues located adjacent to the paramagnetic iron-sulfur cluster.