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2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

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: Homonuclear Correlation Spectroscopy (COSY)01:06

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
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...
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.
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...

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Related Experiment Video

Updated: Jun 10, 2026

Quantitative Magnetic Resonance Imaging of Skeletal Muscle Disease
09:30

Quantitative Magnetic Resonance Imaging of Skeletal Muscle Disease

Published on: December 18, 2016

Doubly sensitivity-enhanced 3D TOCSY-HSQC.

S S Wijmenga1, C P van Mierlo, E Steensma

  • 1SON/NWO National HF-NMR Facility, Nijmegen SON Research Center for Molecular Design, Structure and Synthesis, Toernooiveld, 6525 ED, Nijmegen, The Netherlands.

Journal of Biomolecular NMR
|August 6, 2010
PubMed
Summary
This summary is machine-generated.

This study introduces a doubly enhanced three-dimensional TOCSY-HSQC nuclear magnetic resonance (NMR) sequence. The new method significantly improves signal-to-noise ratios in complex protein analysis, achieving near-theoretical sensitivity enhancements.

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

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

Published on: November 1, 2024

Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Nuclear Magnetic Resonance Spectroscopy

Background:

  • Recent advancements in heteronuclear 3D NMR experiments have focused on sensitivity enhancement strategies.
  • Theoretical sensitivity gains of up to 2^((n-1)/2) are possible for nD spectra.
  • Nuclear Magnetic Resonance (NMR) is a powerful technique for determining molecular structure and dynamics.

Purpose of the Study:

  • To propose and analyze a doubly enhanced three-dimensional (3D) TOCSY-HSQC pulse sequence.
  • To investigate factors contributing to signal-to-noise enhancement in this new NMR sequence.
  • To demonstrate the application of the enhanced sequence for large protein analysis.

Main Methods:

  • Development and theoretical analysis of a doubly enhanced 3D TOCSY-HSQC NMR sequence.
  • Application of the sequence to uniformly (13)C-/(15)N- and (15)N-labeled Azotobacter vinelandii flavodoxin II (179 amino acids).
  • Systematic investigation of factors influencing final signal-to-noise enhancement.

Main Results:

  • The doubly enhanced 3D {(15)N, (1)H} TOCSY-HSQC sequence was successfully applied to a large protein.
  • Sensitivity enhancement achieved was close to the theoretically predicted factor of two compared to standard sequences.
  • Key factors contributing to the overall signal-to-noise enhancement were identified.

Conclusions:

  • The proposed doubly enhanced 3D TOCSY-HSQC sequence provides a significant sensitivity improvement for NMR studies.
  • This technique is effective for analyzing large, isotopically labeled proteins like flavodoxin II.
  • The findings validate the potential of double sensitivity enhancement strategies in multidimensional NMR.