Tolman J R, Flanagan J M, Kennedy M A, Prestegard J H
Department of Chemistry, Yale University, New Haven, CT 06520-8107, USA.
Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9279-83. doi: 10.1073/pnas.92.20.9279.
The measurement of dipolar contributions to the splitting of 15N resonances of 1H-15N 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.
报道了在磁场取向的氰化肌红蛋白的多维高场核磁共振谱中,对1H-15N酰胺对的15N共振分裂的偶极贡献的测量。这些分裂表现为正常标量耦合的小场依赖扰动。将90多个共振分配到蛋白质中特定的序列位点,使得偶极贡献与基于蛋白质已知磁化率和已知结构的预测相关联。讨论了其作为溶液中蛋白质结构测定的额外信息来源的意义。