Oh B H, Westler W M, Darba P, Markley J L
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706.
Science. 1988 May 13;240(4854):908-11. doi: 10.1126/science.3129784.
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, oxidized Anabaena 7120 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.
通过对均匀富集到26%碳-13的蛋白质进行二维双量子碳-13核磁共振实验，借助其一键自旋-自旋耦合识别出直接相连的碳原子网络，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进行分类。通过这种方法识别出了蛋白质氧化鱼腥藻7120铁氧化还原蛋白（分子量11,000）中98个氨基酸残基中的75个自旋系统，这是改进蛋白质核磁共振谱归属方法中的关键一步。缺失的自旋系统主要对应于与顺磁性铁硫簇相邻的残基。
