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Updated: Jul 12, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
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使用加速分子动力学和NMR光谱学探索GB3蛋白质的多个时间尺度运动

Phineus R L Markwick1, Guillaume Bouvignies, Martin Blackledge

  • 1Institute de Biologie Structurale Jean-Pierre Ebel, CNRS, CEA, UJF, UMR 5075, 41 rue Jules Horowitz, F-38027 Grenoble, Cedex, France. phineus@pasteur.fr

Journal of the American Chemical Society
|March 23, 2007
PubMed
概括

加快分子动力学 (AMD) 和NMR揭示了蛋白质G中的复杂蛋白质运动. 这项研究模拟了蛋白质蛋白质.

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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...
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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.