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Updated: Aug 4, 2026

SDS-PAGE/Immunoblot Detection of Aβ Multimers in Human Cortical Tissue Homogenates using Antigen-Epitope Retrieval
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SDS-PAGE/Immunoblot Detection of Aβ Multimers in Human Cortical Tissue Homogenates using Antigen-Epitope Retrieval

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通过固态NMR光谱学捕获阿尔茨海默氏症β-粉样蛋白的中间结构,Abeta(1-40),通过固态NMR光谱学捕获

Sandra Chimon1, Yoshitaka Ishii

  • 1Department of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, USA.

Journal of the American Chemical Society
|September 30, 2005
PubMed
概括

研究人员开发了一种新的固态NMR方法来研究不稳定的粉样中间体,揭示了阿尔茨海默病聚合中的球状结构. 这种技术提供了对神经退行性疾病途径的洞察.

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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NMR Spectroscopy and Mass Spectrometry of Aldehydes and Ketones

In aldehydes, the hydrogen atom connected to the carbonyl carbon helps distinguish aldehydes from other carbonyl compounds using ¹H NMR spectroscopy. The closeness of aldehydic hydrogen to the electrophilic carbonyl carbon highly deshields the hydrogen atom causing its signal to appear around 10 ppm in the ¹H NMR spectra. α hydrogens split the aldehydic proton signal, which helps identify the number of α hydrogens in the molecule. For instance, one α hydrogen creates a doublet for an aldehydic...
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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.