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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

4.8K
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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NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

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In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
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Other Nuclides: 31P, 19F, 15N NMR01:16

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

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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...
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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...
829
Atomic Nuclei: Magnetic Resonance01:05

Atomic Nuclei: Magnetic Resonance

1.4K
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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NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.9K
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...
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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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Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.

Christopher P Jaroniec1

  • 1Department of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH 43210, USA.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|March 24, 2015
PubMed
Summary

Paramagnetism in solid-state NMR provides crucial electron-nucleus distance information beyond traditional methods. This technique is vital for structural studies of biological molecules like proteins.

Keywords:
Magic-angle spinningParamagnetic relaxation enhancementProtein structurePseudocontact shiftSolid-state NMR

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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Solid-state NMR provides insights into molecular structure and dynamics.
  • Paramagnetic effects in NMR offer long-range distance information (∼20 Å).
  • This is particularly useful for biological macromolecules with limited experimental constraints.

Purpose of the Study:

  • To provide an overview of paramagnetic magic-angle spinning NMR applications in biological systems.
  • To highlight investigations of metalloproteins and modified diamagnetic proteins.

Main Methods:

  • Utilizing paramagnetic relaxation enhancements (PREs) and pseudocontact shifts (PCS).
  • Applying magic-angle spinning (MAS) NMR techniques.
  • Employing covalent paramagnetic tags for protein modification.

Main Results:

  • Paramagnetism extends distance measurements significantly beyond nuclear dipolar couplings.
  • This approach enhances structural determination of proteins and biological assemblies.
  • Successful application to both metalloproteins and modified diamagnetic proteins.

Conclusions:

  • Paramagnetic solid-state NMR is a powerful tool for structural biology.
  • It provides valuable long-range distance restraints for complex biological systems.
  • Recent developments enable broader applications to diverse protein types.