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Related Concept Videos

2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

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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...
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2D NMR: Homonuclear Correlation Spectroscopy (COSY)01:06

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

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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...
948
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

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

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

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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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NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

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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...
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¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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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...
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Relaxation-optimized correlation spectroscopy ROCSY for assigning 1H or 13C spin systems in large proteins.

M Rafid Feisal1, Shaista Goel1, Kevin Y L Mak1

  • 1Department of Medicine, University of Alberta, Canada.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|January 3, 2025
PubMed
Summary

We developed Relaxation-Optimized Total Correlation Spectroscopy (ROCSY) to improve Nuclear Magnetic Resonance (NMR) studies of large proteins. ROCSY enhances signal-to-noise by minimizing signal decay, enabling better analysis of complex biological systems.

Keywords:
Protein chemical shift assignmentSolution nuclear magnetic resonance spectroscopyStrong J couplingnuclear Overhauser enhancement (NOE)

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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Nuclear Magnetic Resonance Spectroscopy

Background:

  • Solution Nuclear Magnetic Resonance (NMR) studies of large biomolecules are often limited by rapid signal decay.
  • Signal loss in NMR is primarily due to transverse relaxation and resonance offset effects, complicating the analysis of large systems.

Purpose of the Study:

  • To introduce Relaxation-Optimized Total Correlation Spectroscopy (ROCSY) as a novel NMR technique to enhance signal in large systems.
  • To overcome the limitations of conventional Total Correlation Spectroscopy (TOCSY) by minimizing transverse magnetization duration.

Main Methods:

  • ROCSY utilizes hard pulses within the Clean-CITY TOCSY pulse sequence to maximize magnetization alignment along the z-axis.
  • This approach minimizes transverse relaxation and resonance offset effects, while incorporating through-space Nuclear Overhauser Effect (NOE) for enhanced magnetization transfer.

Main Results:

  • Demonstrated Hα-to-HN correlations in a large integral membrane protein (PagP) using ROCSY, which were not achievable with conventional 1H-TOCSY.
  • Achieved enhanced signal-to-noise ratios compared to 13C-TOCSY for the N-terminal domain of cardiac troponin C.

Conclusions:

  • ROCSY effectively boosts signal in protein NMR experiments employing TOCSY, particularly for higher molecular weight systems.
  • The technique offers a valuable tool for studying large and complex biomolecular systems using NMR spectroscopy.