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Related Concept Videos

Applications Of NMR In Biology01:25

Applications Of NMR In Biology

4.0K
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.
4.0K
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.1K
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...
1.1K
Other Nuclides: 31P, 19F, 15N NMR01:16

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

474
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...
474
Proton (¹H) NMR: Chemical Shift01:07

Proton (¹H) NMR: Chemical Shift

2.0K
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...
2.0K
Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

3.9K
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...
3.9K
¹H NMR: Pople Notation01:09

¹H NMR: Pople Notation

1.9K
The Pople nomenclature system classifies spin systems based on the difference between their chemical shifts. Coupled spins are denoted by capital letters with subscripts indicating the number of equivalent nuclei. When the coupled nuclei have well-separated chemical shifts, they are assigned letters that are far apart in the alphabet, such as A and X. When the difference in chemical shifts is small, coupled nuclei are named using adjacent letters of the alphabet (AB, MN, or XY).
A proton...
1.9K

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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Ion NMR for Biomolecular Systems.

Junji Iwahara1

  • 1Department of Biochemistry & Molecular Biology, Sealy Center for Structural Biology & Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555-1068, USA.

Journal of Molecular Biology
|June 8, 2025
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Summary
This summary is machine-generated.

Nuclear Magnetic Resonance (NMR) methods now reveal dynamic ion behavior around biomolecules. These advances provide new insights into ion interactions with proteins and nucleic acids.

Keywords:
diffusiondynamicselectrostaticsion countingqNMR

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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Biochemistry

Background:

  • Counterions are vital for biomolecular systems, affecting protein and nucleic acid structure and function.
  • Ions are typically not visualized in static biomolecular structures due to dynamic diffusion.
  • Nuclear Magnetic Resonance (NMR) has been used for decades to study ion-biomolecule interactions.

Purpose of the Study:

  • To highlight recent advancements in NMR for studying dynamic ion behavior around biomolecules.
  • To demonstrate the utility of NMR-based diffusion measurements and quantitative NMR (qNMR) for ion analysis.
  • To showcase the application of these NMR techniques to various complex biological systems.

Main Methods:

  • Utilizing advanced NMR probe hardware with strong field gradients for ion diffusion measurements.
  • Applying quantitative NMR (qNMR) to determine ion accumulation around biomolecules.
  • Investigating biologically relevant ions (e.g., 23Na, 25Mg, 31P, 35Cl, 39K) and their interactions.

Main Results:

  • NMR diffusion measurements reveal the high mobility of counterions around biomolecules.
  • Quantitative data on counterion release during protein-DNA association have been obtained.
  • The feasibility of ion NMR has been demonstrated for large biomolecular systems.

Conclusions:

  • Recent NMR advances enable detailed investigation of dynamic ion behavior around biomolecules.
  • NMR-based diffusion and qNMR are powerful tools for understanding ion-biomolecule electrostatics.
  • These methods offer promising applications for studying complex biological systems and processes.