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Related Concept Videos

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.
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: 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...
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...
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.
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...

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In Situ Monitoring of Diffusion of Guest Molecules in Porous Media Using Electron Paramagnetic Resonance Imaging
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Measuring macromolecular diffusion using heteronuclear multiple-quantum pulsed-field-gradient NMR.

A J Dingley1, J P Mackay, G L Shaw

  • 1Department of Biochemistry, University of Sydney, Sydney, NSW, 2006, Australia.

Journal of Biomolecular NMR
|August 5, 2010
PubMed
Summary
This summary is machine-generated.

This study introduces enhanced pulsed-field-gradient (PFG) NMR methods using (1)H-(15)N multiple-quantum coherences for improved protein self-association monitoring. These advanced techniques facilitate more accurate measurement of diffusion coefficients for larger biomolecules.

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Area of Science:

  • Biophysical Chemistry
  • Nuclear Magnetic Resonance Spectroscopy
  • Protein Science

Background:

  • Pulsed-field-gradient (PFG) NMR spectroscopy is established for monitoring protein self-association and estimating molecular mass.
  • Traditional (1)H single-quantum (SQ) magnetization methods have limitations in sensitivity and applicability to larger proteins.

Purpose of the Study:

  • To present an improved PFG NMR methodology utilizing (1)H-(15)N multiple-quantum (MQ) coherences for protein analysis.
  • To overcome the limitations of SQ methods in measuring diffusion coefficients of larger proteins and enhance signal suppression.

Main Methods:

  • Implementation of a gradient-selected MQ filter to suppress solvent and unlabeled solute resonances.
  • Utilizing the faster dephasing of (1)H-(15)N zero-quantum coherence compared to (1)H SQ coherence under PFG.
  • Development of a novel MQ PFG diffusion experiment storing magnetization as longitudinal two-spin order to minimize sensitivity losses.

Main Results:

  • Demonstrated advantages of (1)H-(15)N MQ coherences over (1)H SQ magnetization in PFG diffusion experiments.
  • Enabled more facile measurement of diffusion coefficients for larger proteins.
  • Reduced signal loss from relaxation and J-coupling evolution, extending applicability to larger macromolecules.

Conclusions:

  • The developed (1)H-(15)N MQ PFG NMR techniques offer significant improvements for studying protein self-association and diffusion.
  • These methods provide enhanced sensitivity and broader applicability for analyzing larger protein systems.
  • The new approach minimizes sensitivity losses, making it a powerful tool in biophysical characterization.