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Related Concept Videos

Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

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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...
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Magnetic Resonance Imaging01:24

Magnetic Resonance Imaging

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Magnetic resonance imaging (MRI) is a noninvasive medical imaging technique based on a phenomenon of nuclear physics discovered in the 1930s, in which matter exposed to magnetic fields and radio waves was found to emit radio signals. In 1970, a physician and researcher named Raymond Damadian noticed that malignant (cancerous) tissue gave off different signals than normal body tissue. He applied for a patent for the first MRI scanning device in clinical use by the early 1980s. The early MRI...
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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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Atomic Nuclei: Nuclear Magnetic Moment00:59

Atomic Nuclei: Nuclear Magnetic Moment

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All atomic nuclei are positively charged. When they have a nonzero spin, they behave like rotating charges. As a consequence of their charge and spin, these nuclei generate a magnetic field (B). This, in turn, gives rise to a magnetic moment (μ), which is randomly oriented in the absence of an external magnetic field. When an external magnetic field (B0) is applied, the magnetic moment vectors can align with the field or against it in 2 + 1 orientations. A hydrogen nucleus, which is just a...
3.3K
Nuclear Fusion02:45

Nuclear Fusion

33.8K
The process of converting very light nuclei into heavier nuclei is also accompanied by the conversion of mass into large amounts of energy, a process called fusion. The principal source of energy in the sun is a net fusion reaction in which four hydrogen nuclei fuse and ultimately produce one helium nucleus and two positrons.
A helium nucleus has a mass that is 0.7% less than that of four hydrogen nuclei; this lost mass is converted into energy during the fusion. This reaction produces about...
33.8K
Resonance02:52

Resonance

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The Lewis structure of a nitrite anion (NO2−) may actually be drawn in two different ways, distinguished by the locations of the N-O and N=O bonds.
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Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
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Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

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View from Nuclear Magnetic Resonance Spectroscopy.

John L Markley1

  • 1Biochemistry Department, University of Wisconsin-Madison, Madison, WI, USA. jmarkley@wisc.edu.

Advances in Experimental Medicine and Biology
|January 9, 2019
PubMed
Summary

Nuclear magnetic resonance (NMR) spectroscopy is a key method for determining macromolecular structures, excelling in studying protein dynamics. It complements other techniques like CryoEM and X-ray crystallography.

Keywords:
Data visualizationNMRSpectral assignmentStructure determination

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Nuclear magnetic resonance (NMR) spectroscopy is a primary technique for elucidating biological macromolecular structures.
  • Historically second to X-ray crystallography in Protein Data Bank (PDB) depositions, NMR's role has evolved with advancements in electron cryomicroscopy (CryoEM).
  • NMR is often integrated with X-ray crystallography and CryoEM for comprehensive structure determination.

Purpose of the Study:

  • To highlight the unique advantages of NMR spectroscopy in structural biology.
  • To discuss the synergistic relationship between NMR and other structural methods, particularly CryoEM.
  • To emphasize NMR's utility in studying dynamic processes and conformational heterogeneity in biomolecules.

Main Methods:

  • NMR spectroscopy utilizes multiple magnetic resonance experiments to determine nuclear connectivities and dipole orientations.
  • Data from NMR experiments are integrated with other biophysical methods like small-angle X-ray scattering and chemical crosslinking.
  • NMR does not require sample crystallization, a significant advantage shared with CryoEM.

Main Results:

  • NMR spectroscopy provides crucial insights into conformational dynamics and interconverting states of proteins and nucleic acids in solution.
  • NMR results, when combined with other data, contribute to robust structural models.
  • The non-crystallization requirement of NMR makes it highly compatible with CryoEM.

Conclusions:

  • NMR spectroscopy remains an indispensable tool in structural biology, particularly for dynamic studies.
  • The integration of NMR with techniques like CryoEM offers powerful, complementary approaches to structure determination.
  • NMR's ability to study molecules in solution and its synergy with CryoEM enhance structural biology research.