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2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...

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Related Experiment Video

Updated: May 13, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

NMR ¹⁵N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Solid-state NMR spectroscopy of proteins.

Henrik Müller¹, Manuel Etzkorn, Henrike Heise

¹Institute of Physical Biology, Heinrich-Heine-University of Düsseldorf, 40225, Düsseldorf, Germany.

Topics in Current Chemistry

|March 19, 2013

Summary

Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique for studying complex biological molecules. Magic Angle Spinning (MAS) NMR advances protein structure determination, addressing current challenges and recent progress.

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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

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Last Updated: May 13, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

NMR ¹⁵N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

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:

Biochemistry
Biophysics
Spectroscopy

Background:

Solid-state NMR spectroscopy is a versatile tool for characterizing complex biochemical systems.
Magic Angle Spinning (MAS) solid-state NMR has matured for structural elucidation of biological macromolecules.

Purpose of the Study:

Discuss current challenges in applying solid-state NMR.
Highlight recent progress in the field.
Focus on conceptual aspects for protein structural elucidation.

Main Methods:

Solid-state NMR spectroscopy.
Magic Angle Spinning (MAS) technique.

Main Results:

Demonstrated the versatility of solid-state NMR for structure and dynamics.
Highlighted the maturity of MAS NMR for macromolecular structural elucidation.

Conclusions:

Solid-state NMR, particularly MAS NMR, is crucial for understanding protein structures.
Ongoing advancements continue to improve its application in structural biology.