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Updated: Mar 1, 2026

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
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时间解析的SAXS揭示了单体α-Synuclein的明显的毫秒金属诱导的形态动力学

Rebecca Sternke-Hoffmann1, Miriam Dos Santos Pinto1, Xue Wang1

  • 1PSI Center for Life Sciences, Villigen PSI, Switzerland.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)
|February 28, 2026
PubMed
概括

铁和铜等金属离子迅速改变α-synuclein结构,影响帕金森氏症.

关键词:
构造动力学 构造动力学本质上是无序的蛋白质.金属离子金属离子蛋白质与金属的相互作用时间解决的SAXS.α-synuclein 是一种同核蛋白.

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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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