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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

4.4K
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.
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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...
1.1K
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

1.0K
When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
1.0K
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

2.9K
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...
2.9K
Other Nuclides: 31P, 19F, 15N NMR01:16

Other Nuclides: 31P, 19F, 15N NMR

703
Many organic, inorganic, and biological molecules contain spin-half nuclei such as nitrogen-15, fluorine-19, and phosphorus-31. As a result, NMR studies of these nuclei have found extensive applications in chemical and biological research.
While fluorine-19 and phosphorous-31 have high natural abundances (100%) and positive gyromagnetic ratios, nitrogen-15 has a low natural abundance and a negative gyromagnetic ratio. However, nitrogen-15 is still preferred over nitrogen-14 (which has a...
703
Proton (¹H) NMR: Chemical Shift01:07

Proton (¹H) NMR: Chemical Shift

3.2K
Organic molecules primarily contain carbon and hydrogen atoms. While all the hydrogen isotopes are NMR-active, protium or hydrogen-1 is the most abundant. It has a significant energy separation between its nuclear spin states due to its large gyromagnetic ratio. As per Boltzmann's distribution, an increase in the energy separation implies a greater excess population of nuclei available for excitation, resulting in a strong NMR absorption signal.
Absorption signals of all the protium nuclei...
3.2K

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Updated: Jan 6, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Paramagnetic solid-state NMR of proteins.

Ming Tang1, Dennis Lam1

  • 1Department of Chemistry, College of Staten Island - Ph.D. Programs in Chemistry and Biochemistry, The Graduate Center of the City University of New York, New York, NY, 10016, USA.

Solid State Nuclear Magnetic Resonance
|October 6, 2019
PubMed
Summary
This summary is machine-generated.

Paramagnetic effects from metal ions and radicals offer new ways to study proteins using solid-state NMR. This technique enhances sensitivity and aids in determining the structure of various protein types.

Keywords:
Amyloid fibrilsMembrane proteinsMicrocrystalline proteinsParamagnetic relaxation effectProtein aggregatesProtein complexesPseudo-contact shiftSolid-state NMR

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Area of Science:

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

Background:

  • Paramagnetic properties of metal ions and stable radicals influence Nuclear Magnetic Resonance (NMR) spectra.
  • These paramagnetic effects can alter peak intensities, relaxation times, and chemical shifts in NMR spectra.
  • Such alterations present unique opportunities for advanced solid-state NMR studies of proteins.

Purpose of the Study:

  • To review trends and progress in paramagnetic solid-state NMR of proteins over the last decade.
  • To highlight the potential applications of paramagnetic effects in protein structural analysis.
  • To showcase the utility of paramagnetic solid-state NMR for various protein systems.

Main Methods:

  • Review of recent literature on paramagnetic solid-state NMR of proteins.
  • Analysis of paramagnetic effects on NMR spectral parameters (intensity, relaxation, chemical shift).
  • Application of paramagnetic solid-state NMR to microcrystalline proteins, complexes, aggregates, and membrane proteins.

Main Results:

  • Paramagnetic effects provide significant potential for sensitivity enhancement in solid-state NMR.
  • These effects are valuable for accurate structure determination of proteins.
  • Paramagnetic solid-state NMR enables detailed topological analysis of complex protein assemblies.

Conclusions:

  • Paramagnetic solid-state NMR is a powerful technique for protein structure and dynamics.
  • The method shows great promise for studying challenging protein systems, including aggregates and membrane proteins.
  • Continued advancements in paramagnetic solid-state NMR will further expand its applications in structural biology.