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通过¹H纵向自旋弛豫研究蛋白质酰胺质子交换

Investigation of protein amide-proton exchange by 1H longitudinal spin relaxation.

作者信息

Zheng Z, Gryk M R, Finucane M D, Jardetzky O

机构信息

Stanford Magnetic Resonance Laboratory, Stanford University, California 94305-5055, USA.

出版信息

J Magn Reson B. 1995 Sep;108(3):220-34. doi: 10.1006/jmrb.1995.1127.

Abstract

The general theory of the Linderstrøm-Lang model, which, in simplified form, is widely used for the interpretation of NMR data on backbone-proton exchange in proteins, is systematically discussed. An experimental protocol for testing the applicability of the customary simplifications is described and experimental data which require the application of the general, rather than of the simplified, theory are presented. The appearance of pH-dependent biexponential magnetization recovery for any amide group in a protein is an unequivocal indication that the conventional simplified versions of the model do not apply.

摘要

林德斯特伦 - 朗模型的一般理论(其简化形式被广泛用于解释蛋白质主链质子交换的核磁共振数据)得到了系统讨论。描述了一种用于测试常规简化方法适用性的实验方案,并给出了需要应用一般理论而非简化理论的实验数据。蛋白质中任何酰胺基团出现pH依赖的双指数磁化恢复现象明确表明该模型的传统简化版本不适用。

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