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Updated: Aug 11, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

通过乳NMR自旋放松探测高分子量蛋白质的侧链动态:对82kDa酶的应用

Vitali Tugarinov1, Jason E Ollerenshaw, Lewis E Kay

  • 1Protein Engineering Network Centers of Excellence and Department of Medical Genetics, The University of Toronto, Toronto, Ontario M5S 1A8, Canada.

Journal of the American Chemical Society
|June 2, 2005
PubMed
概括

新的NMR实验可以详细研究大分子中蛋白质侧链动态. 这种方法提高了研究蛋白质运动和结构的灵敏度和分辨率.

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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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¹H NMR of Labile Protons: Deuterium (²H) Substitution

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