Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets

Journal of Magnetic Resonance (1969) Pub Date : 1992-10-01 DOI:10.1016/0022-2364(92)90209-P

T Szyperski, P Güntert, G Otting, K Wüthrich

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引用次数: 153

Abstract

A generally applicable new method for the determination of scalar coupling constants for spins with a single coupling partner, in particular ³J_HNα. in polypeptides, is described. It has the special advantage for use in protein structure determinations that no extra NMR experiments need to be recorded, and that NOE distance constraints and dihedral angle constraints from ³J_HNα can be derived from the same data sets. The scalar coupling constants are extracted from the in-phase multiplets of homonuclear [¹H, ¹H] NOESY spectra or heteronuclear [¹⁵N, ¹H ] COSY spectra through inverse Fourier transformation of the data points representing a cross peak along ω₂, and a subsequent nonlinear least-squares fit in the time domain. Practical applications are described for recombinant hirudin and the basic pancreatic trypsin inhibitor.

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用同相多态傅里叶反变换确定标量耦合常数

一种确定具有单一耦合伙伴的自旋标量耦合常数的普遍适用的新方法，特别是3JHNα。在多肽中，被描述。它在蛋白质结构测定中具有特殊的优势，即不需要记录额外的核磁共振实验，并且可以从相同的数据集推导出3JHNα的NOE距离约束和二面角约束。从同核[1H, 1H] NOESY光谱或异核[15N, 1H] COSY光谱的同相多重波中提取标量耦合常数，对沿ω2的交叉峰数据点进行傅里叶反变换，并在时域进行非线性最小二乘拟合。介绍了重组水蛭素和碱性胰蛋白酶抑制剂的实际应用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Journal of Magnetic Resonance (1969)

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