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Updated: Jun 13, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
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直接使用15N放松率作为对蛋白质-蛋白质复合体对接的分子形状和方向的实验限制

Yaroslav Ryabov1, G Marius Clore, Charles D Schwieters

  • 1Division of Computational Bioscience, Building 12A, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 20892-5624, USA.

Journal of the American Chemical Society
|April 16, 2010
PubMed
概括

一种新方法使用-15 (15N) 放松率直接计算蛋白质结构和复合体. 这种方法有助于确定分子形状和方向,而不需要先前存在的结构.

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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...