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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 broad and...

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Related Experiment Video

Updated: May 31, 2026

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

Solid-state NMR sequential assignments of α-synuclein.

Julia Gath¹, Birgit Habenstein, Luc Bousset

¹Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zurich, Switzerland.

Biomolecular NMR Assignments

|July 12, 2011

Summary

This summary is machine-generated.

Researchers characterized a new form of alpha-synuclein protein fibrils, crucial in Parkinson's disease. This finding offers structural insights into protein aggregation in neurodegenerative diseases.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Area of Science:

Neuroscience
Biochemistry
Structural Biology

Background:

Parkinson's disease is a common neurodegenerative disorder linked to protein aggregation.
Alpha-synuclein protein accumulation forms Lewy bodies in affected brains.
Protein species assembly and intercellular propagation are key pathological mechanisms.

Purpose of the Study:

To determine the solid-state NMR sequential assignments for a novel fibrillar form of alpha-synuclein.
To characterize the structural properties of this new fibril, particularly its N-terminal region.

Main Methods:

Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy was employed.
Sequential assignments were obtained for the alpha-synuclein fibril.
Structural analysis focused on the N-terminal segment of the protein.

Main Results:

The study presents the first solid-state NMR sequential assignments for this specific fibrillar form of alpha-synuclein.
This new fibril exhibits a well-ordered and rigid N-terminal region.
The findings provide detailed structural information about alpha-synuclein aggregation.

Conclusions:

The characterized alpha-synuclein fibril represents a distinct structural polymorph.
The rigid N-terminal structure may influence fibril formation and propagation.
This structural data is vital for understanding Parkinson's disease pathogenesis and developing therapeutic strategies.