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Related Concept Videos

2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

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...
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

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 in...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

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.
The...
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

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...

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Updated: May 18, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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

Published on: September 17, 2017

High-resolution structural insights into bone: a solid-state NMR relaxation study utilizing paramagnetic doping.

Kamal H Mroue1, Neil MacKinnon, Jiadi Xu

  • 1Biophysics, The University of Michigan, Ann Arbor, Michigan 48109-1055, USA.

The Journal of Physical Chemistry. B
|September 8, 2012
PubMed
Summary
This summary is machine-generated.

This study uses copper(II) ions to significantly reduce the data collection time for solid-state nuclear magnetic resonance (SSNMR) of bone. This acceleration allows for faster atomic-level structural studies of bone and biomaterials.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Area of Science:

  • Biophysics
  • Materials Science
  • Biomaterials

Background:

  • Bone's complex structure challenges traditional biophysical studies.
  • High-resolution solid-state nuclear magnetic resonance (SSNMR) offers atomic-level insights but suffers from long data acquisition times.
  • Shortening relaxation times is key to improving SSNMR efficiency for bone research.

Purpose of the Study:

  • To accelerate SSNMR data acquisition for bone and biomaterials.
  • To investigate the use of copper(II) ions to shorten proton spin-lattice (T(1)) relaxation times.
  • To assess the impact of paramagnetic relaxation enhancement on spectral resolution and data collection.

Main Methods:

  • Solid-state (13)C cross-polarization magic-angle-spinning (CPMAS) NMR experiments were performed on bone samples.
  • Proton (1)H T(1) relaxation times were measured in the presence and absence of Cu(II)(NH(4))(2)EDTA.
  • Experiments were conducted on type I collagen, bovine cortical bone, and demineralized bovine cortical bone.

Main Results:

  • (1)H T(1) relaxation times were reduced by factors of 2.2 to 3.2 across different bone samples.
  • Spectral resolution was maintained, enabling faster data acquisition.
  • Paramagnetic quenching of specific (13)C resonances suggested proximity of certain amino acids to bone mineral.

Conclusions:

  • Copper(II) ion-induced paramagnetic relaxation effectively shortens SSNMR acquisition times for bone.
  • This method enhances the feasibility of SSNMR for studying bone structure and dynamics.
  • The findings may offer insights into the interaction between bone matrix components and mineral surfaces.