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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...

2D NMR: Overview of Heteronuclear Correlation Techniques

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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.

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Related Experiment Video

Updated: May 26, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Hsp90 structure and function studied by NMR spectroscopy.

Tatiana Didenko¹, Afonso M S Duarte, G Elif Karagöz

¹Utrecht University, Utrecht, the Netherlands.

Biochimica Et Biophysica Acta

|December 14, 2011

Summary

Nuclear magnetic resonance (NMR) spectroscopy advances the study of Heat Shock Protein 90 (Hsp90) mechanisms. This technique reveals Hsp90

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Heat Shock Protein 90 (Hsp90) is a molecular chaperone vital for protein folding and maturation.
Hsp90's ATPase cycle and substrate interactions are not fully understood.
Protein flexibility and high molecular weight challenge structural studies of Hsp90.

Purpose of the Study:

To explore the application of advanced Nuclear Magnetic Resonance (NMR) spectroscopy for investigating Hsp90.
To elucidate Hsp90's dynamic mechanisms and interactions with co-chaperones and client proteins.
To overcome traditional limitations in studying large, flexible proteins like Hsp90.

Main Methods:

Utilized state-of-the-art Nuclear Magnetic Resonance (NMR) spectroscopy techniques.

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Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Published on: January 30, 2018

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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Published on: January 30, 2018

Applied NMR to study Hsp90's interactions with co-chaperones (p23, Aha1, Cdc37).

Investigated Hsp90's interaction with the client protein, tumor suppressor p53, using NMR.

Main Results:

NMR spectroscopy provided insights into Hsp90's interactions with co-chaperones.
Demonstrated NMR's capability in characterizing interactions with substrate proteins, including p53.
Highlighted NMR's suitability for studying dynamic protein-protein interactions at atomic resolution.

Conclusions:

Advanced NMR methods are effective for studying the challenging Hsp90 chaperone system.
NMR spectroscopy is crucial for understanding Hsp90's mechanism, co-chaperone binding, and client interactions.
This approach offers a dynamic view of protein interactions, particularly for partially folded substrates like p53.