Logan T M, Olejniczak E T, Xu R X, Fesik S W
Pharmacuetical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064.
FEBS Lett. 1992 Dec 21;314(3):413-8. doi: 10.1016/0014-5793(92)81517-p.
Two multi-dimensional heteronuclear NMR experiments are described for assigning the resonances in uniformly 15N- and 13C-labeled proteins. In one experiment (HCNH-TOCSY), the amide nitrogen and proton are correlated to the side-chain protons and carbons of the same and preceding residue. In a second triple resonance experiment (HC(CO)NH-TOCSY), the amide nitrogen and proton of one residue is correlated exclusively with the side-chain proton and carbon resonances of the preceding residue by transferring magnetization through the intervening carbonyl. The utility of these two experiments for making sequential resonance assignments in proteins is illustrated for [U-15N,13C]FKBP (107 residues) complexed to the immunosuppressant, ascomycin.
描述了两种用于确定均匀15N和13C标记蛋白质中各共振峰归属的多维异核核磁共振实验。在一个实验（HCNH-TOCSY）中，酰胺氮和质子与同一残基及前一个残基的侧链质子和碳相关联。在第二个三重共振实验（HC(CO)NH-TOCSY）中，一个残基的酰胺氮和质子通过经中间羰基传递磁化，仅与前一个残基的侧链质子和碳共振峰相关联。对于与免疫抑制剂子囊霉素复合的[U-15N,13C]FKBP（107个残基），展示了这两个实验在蛋白质序列共振归属方面的实用性。
