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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

3.7K
Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
3.7K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

1.2K
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...
1.2K
Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

619
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...
619
Diamagnetic Shielding of Nuclei: Local Diamagnetic Current01:14

Diamagnetic Shielding of Nuclei: Local Diamagnetic Current

822
An applied magnetic field causes the electrons present in the molecule to circulate, setting up a local diamagnetic current within the molecule. The local diamagnetic current arising from circulating sigma-bonding electrons induces a magnetic field, Blocal that opposes the applied magnetic field, B0. The effective magnetic field experienced by these nuclei is given by the difference between the applied and local magnetic fields in a phenomenon called local diamagnetic shielding. Essentially,...
822
Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

2.1K
Nuclear magnetic resonance (NMR) is a phenomenon exhibited by certain nuclei that can absorb characteristic radio frequency radiation under certain conditions. NMR has been extensively applied in molecular spectroscopy and medical diagnostic imaging. In both these applications, the molecule or subject under study is placed in a magnetic field and irradiated with radio frequency energy.
NMR spectroscopy generates a spectrum where the characteristic absorption frequencies of the sample are...
2.1K
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.0K
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...
1.0K

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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.

Hannah Busch1, Muhammad Yasir Ateeque2, Florian Taube3

  • 1Institute of Technical and Macromolecular Chemistry, RWTH Aachen University, Worringerweg 2, 52074, Aachen, Germany.

Chembiochem : a European Journal of Chemical Biology
|January 13, 2025
PubMed
Summary

Nuclear Magnetic Resonance (NMR) spectroscopy, especially paramagnetic NMR, provides crucial insights into complex protein structures. Combining NMR with AlphaFold enhances the study of biomolecular interactions.

Keywords:
Biomolecular interactionsdynamic nuclear polarizationparamagnetic NMRparamagnetic relaxation enhancementpseudocontact shifts

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Area of Science:

  • Structural biology
  • Biophysics
  • Computational biology

Background:

  • AlphaFold revolutionized protein structure prediction but struggles with dynamic or disordered systems.
  • Nuclear Magnetic Resonance (NMR) spectroscopy offers atomic-level detail for weakly interacting and dynamic biomolecular complexes.
  • Paramagnetic NMR provides long-range distance restraints, ideal for large protein complexes.

Purpose of the Study:

  • To review paramagnetic NMR approaches for analyzing biomolecular complexes in solution and solid states.
  • To highlight the utility of paramagnetic NMR in conjunction with advances in chemical tagging and EPR spectroscopy.
  • To discuss the integration of computational methods like AlphaFold with experimental NMR data.

Main Methods:

  • Paramagnetic NMR spectroscopy, including pseudocontact shifts, residual dipolar couplings, and paramagnetic relaxation enhancements.
  • Advanced chemical methods for introducing paramagnetic tags into proteins.
  • Electron Paramagnetic Resonance (EPR) spectroscopy.
  • Dynamic Nuclear Polarization (DNP) for signal enhancement.

Main Results:

  • Paramagnetic NMR yields long-range structural restraints (>25 Å) for large and dynamic protein complexes.
  • Advances in tagging and EPR enhance the applicability of paramagnetic NMR.
  • Dynamic Nuclear Polarization significantly amplifies NMR signals, aiding the study of large complexes.

Conclusions:

  • Paramagnetic NMR is a powerful technique for characterizing complex biomolecular systems.
  • Integration of AlphaFold predictions with paramagnetic NMR data holds significant potential for advancing structural biology.
  • This combined approach promises deeper understanding of biomolecular interactions and mechanisms.