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Updated: Jun 7, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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优化的测量温度可以访问49 kDa的同质美式β螺旋的溶液结构

Ilka Varnay1, Vincent Truffault, Sergej Djuranovic

  • 1Institute for Advanced Study and Center of Integrated Protein Science, Department Chemie, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany.

Journal of the American Chemical Society
|October 22, 2010
PubMed
概括

研究人员使用高温NMR确定了Pyrococcus horikoshii中大型蛋白质域 (Ph1500C) 的高分辨率结构. 这种方法使得这种具有挑战性的蛋白质能够进行详细的结构分析,从而推进了超热友的古研究.

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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

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.