NUCLEAR MAGNETIC DIPOLE INTERACTIONS IN FIELD-ORIENTED PROTEINS - INFORMATION FOR STRUCTURE DETERMINATION IN SOLUTION
NUCLEAR MAGNETIC DIPOLE INTERACTIONS IN FIELD-ORIENTED PROTEINS - INFORMATION FOR STRUCTURE DETERMINATION IN SOLUTION
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DOI：
10.1073/pnas.92.20.9279
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发表时间：
1995-09-26
影响因子：
11.1
通讯作者：
PRESTEGARD, JH
中科院分区：
文献类型：
--
作者：
TOLMAN, JR;FLANAGAN, JM;PRESTEGARD, JH
本文报道了偶极对场取向氰高铁肌红蛋白多维高场NMR谱中H-1-N-15酰胺对N-15共振分裂的贡献。分裂表现为正常标量耦合的小场相关扰动。分配超过90个共振到蛋白质中的特定顺序位点允许偶极贡献与基于蛋白质的已知磁化率和已知结构的预测的相关性。作为一个额外的信息来源，在溶液中的蛋白质结构测定的影响进行了讨论。
The measurement of dipolar contributions to the splitting of N-15 resonances of H-1-N-15 amide pairs in multidimensional high-field NMR spectra of field-oriented cyanometmyoglobin is reported. The splittings appear as small field dependent perturbations of normal scalar couplings. Assignment of more than 90 resonances to specific sequential sites in the protein allows correlation of the dipolar contributions with predictions based on the known susceptibility and known structure of the protein. Implications as an additional source of information for protein structure determination in solution are discussed.