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Related Concept Videos

¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
Carbon-13 (¹³C) NMR: Overview01:10

Carbon-13 (¹³C) NMR: Overview

Carbon-13 is a naturally occurring NMR-active isotope of carbon with a low natural abundance of 1.1%. In contrast, carbon-12 is the most abundant isotope of carbon with zero nuclear spin. Therefore, it is NMR inactive. The gyromagnetic ratio of carbon-13 is smaller than that of protons. As a result, carbon-13 resonance is about 6000 times weaker than proton resonance. For a given magnetic field strength, the resonance frequency of carbon-13 is about one-fourth of the resonance frequency for...
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved in...
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other axis.
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...

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Updated: Jun 8, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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

Published on: September 17, 2017

Supramolecular interactions probed by 13C-13C solid-state NMR spectroscopy.

Antoine Loquet1, Karin Giller, Stefan Becker

  • 1Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.

Journal of the American Chemical Society
|October 12, 2010
PubMed
Summary

We developed a solid-state NMR method to study protein interfaces in insoluble complexes. This technique revealed that Parkinson's disease-associated alpha-synuclein fibrils stack in a parallel in-register arrangement.

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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

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Last Updated: Jun 8, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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

Published on: September 17, 2017

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Protein-protein interactions are crucial for cellular function.
  • Insoluble and noncrystalline protein aggregates, like those in neurodegenerative diseases, present challenges for structural determination.
  • Understanding the structure of alpha-synuclein fibrils is key to Parkinson's disease research.

Purpose of the Study:

  • To develop a robust solid-state NMR method for determining molecular interfaces in insoluble protein complexes.
  • To elucidate the structural arrangement of alpha-synuclein fibrils associated with Parkinson's disease.

Main Methods:

  • Utilized solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Measured intermolecular carbon-13 (13C)–carbon-13 (13C) distances.
  • Employed mixtures of [1-(13)C]glucose- and [2-(13)C]glucose-labeled proteins.

Main Results:

  • Successfully determined molecular interfaces in insoluble and noncrystalline protein-protein complexes.
  • Established that alpha-synuclein fibrils are arranged in a parallel in-register manner.
  • Collected intermolecular distance restraints enabling atomic-resolution structure determination of the fibrils.

Conclusions:

  • The developed solid-state NMR approach is effective for characterizing challenging protein assemblies.
  • The parallel in-register stacking of alpha-synuclein fibrils provides new insights into Parkinson's disease pathogenesis.
  • This method facilitates high-resolution structural studies of amyloid fibrils.