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Related Concept Videos

NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

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In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
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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.
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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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Related Experiment Video

Updated: Jun 22, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Solid-state NMR assignment of α-synuclein polymorph prepared from helical intermediate.

Sahil Ahlawat1, Surabhi Mehra2, Chandrakala M Gowda3

  • 1Tata Institute of Fundamental Research, Sy. No. 36/P, Gopanpally Village, Serilingampally Mandal, Ranga Reddy District, Hyderabad, 500 046, India. sahilr@tifrh.res.in.

Biomolecular NMR Assignments
|July 4, 2024
PubMed
Summary

Synucleinopathies involve alpha-synuclein protein aggregates. This study reveals distinct alpha-synuclein fibril structures (polymorphs) arising from different protein intermediates, potentially explaining varied disease pathologies.

Keywords:
AssignmentFibrilsOligomersSolid-state NMRα–Synuclein

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Synucleinopathies are neurodegenerative diseases defined by alpha-synuclein protein aggregate accumulation.
  • Alpha-synuclein fibrils exhibit polymorphism, meaning structural variations can arise from a single protein.
  • These structural variations (polymorphs) may correlate with distinct biophysical, biochemical, and pathogenic properties, potentially explaining disease heterogeneity.

Purpose of the Study:

  • To investigate the hypothesis that different alpha-synuclein polymorphs arise from distinct intermediate structures during fibril formation.
  • To characterize the structure of alpha-synuclein fibrils formed from a specific helical intermediate.

Main Methods:

  • In vitro fibrillization of alpha-synuclein.
  • Isolation and incubation of specific protein intermediates.
  • Solid-state nuclear magnetic resonance (NMR) spectroscopy, including 13C and 15N chemical shift analysis.
  • Determination of secondary structure.

Main Results:

  • Successfully prepared alpha-synuclein fibrils from a helical intermediate.
  • Reported 13C and 15N chemical shifts for these fibrils.
  • Determined the secondary structure of the fibrils derived from the helical intermediate.

Conclusions:

  • The study provides structural insights into alpha-synuclein polymorphs derived from specific intermediates.
  • This work contributes to understanding the structural basis of synucleinopathy diversity.
  • Solid-state NMR is a valuable tool for characterizing fibril structures in neurodegenerative diseases.