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Related Concept Videos

Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

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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...
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Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

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The number of nuclear spins aligned in the lower energy state is slightly greater than those in the higher energy state. In the presence of an external magnetic field, as the spins precess at the Larmor frequency, the excess population results in a net magnetization oriented along the z axis. When a pulse or a short burst of radio waves at the Larmor frequency is applied along the x axis, the coupling of frequencies causes resonance and flips the nuclear spins of the excess population from the...
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¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

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

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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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¹H NMR: Interpreting Distorted and Overlapping Signals01:02

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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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Insensitive Nuclei Enhanced by Polarization Transfer (INEPT)01:15

Insensitive Nuclei Enhanced by Polarization Transfer (INEPT)

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Insensitive Nuclei Enhanced by Polarization Transfer (INEPT) is an advanced Nuclear Magnetic Resonance (NMR) technique specifically designed to detect and enhance the signals of low-abundance nuclei, such as carbon-13 and nitrogen-15, in small molecules. The fundamental principle behind INEPT is the transfer of polarization from a more abundant and highly polarizable nucleus, typically hydrogen-1, to the low-abundance nucleus of interest. This process effectively boosts the NMR signal of the...
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Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

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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.
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Quantitative Magnetic Resonance Imaging of Skeletal Muscle Disease
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Transferred-Rotational-Echo Double Resonance.

Xizhou Cecily Zhang1, Marcel C Forster1, Evgeny Nimerovsky1

  • 1NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Faßberg 11, 37077 Göttingen, Germany.

The Journal of Physical Chemistry. A
|January 19, 2021
PubMed
Summary
This summary is machine-generated.

A new method, transferred-rotational-echo double resonance (TREDOR), enables faster and more precise internuclear distance measurements for nuclear magnetic resonance (NMR) structure calculations. This technique significantly reduces data acquisition time, making it suitable for complex molecules.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Internuclear distance measurement is crucial for NMR-based structure calculation.
  • Current methods are time-consuming, limiting applications to large or complex molecular systems.

Purpose of the Study:

  • To introduce a novel heteronuclear transfer method, transferred-rotational-echo double resonance (TREDOR).
  • To demonstrate TREDOR's efficiency and accuracy in determining internuclear distances and calculating molecular structures.

Main Methods:

  • Developed and applied the TREDOR technique for simultaneous detection of starting and transferred signals in a single spectrum.
  • Utilized 3D spectra for resonance resolution in microcrystalline SH3 protein.
  • Combined N-C and H-C distances for structure calculation.

Main Results:

  • TREDOR allows accurate and precise distance determination via a single parameter fit from a single spectrum.
  • Achieved structure calculation of SH3 protein with a root-mean-square deviation of 2.1 Å compared to X-ray structure.
  • Acquired data in only 4 days on a 600 MHz instrument, demonstrating a >2-fold time saving.

Conclusions:

  • TREDOR significantly accelerates NMR structure determination by compensating for coherence decay through signal co-acquisition.
  • Presents TREDOR as a fast and straightforward method for magic-angle spinning NMR structure determination, applicable to challenging systems.