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Related Concept Videos

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...
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2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

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Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other...
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2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

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Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
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¹H NMR Signal Multiplicity: Splitting Patterns01:13

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When protons A and X are coupled, their nuclear spin energy levels are slightly modified. This is because the energy required to excite proton A to a spin state parallel to proton X is slightly different from the energy required for it to become anti-parallel to spin X. Consequently, there are two possible excitation frequencies for A (A1 and A2), depending on the spin state of X, and vice versa. The mutual nature of coupling implies that the difference between frequencies A1 and A2, indicated...
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Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
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Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

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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.
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Probing Spatial Proximities Between Protons of Collagen Protein in Native Bone Using 2D 1H Multiple Quantum

Bijaylaxmi Patra1,2, Vipin Agarwal3, Yusuke Nishiyama4

  • 1Centre of Biomedical Research, Lucknow, India.

Magnetic Resonance in Chemistry : MRC
|January 2, 2025
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Summary

Fast magic angle spinning (MAS) solid-state nuclear magnetic resonance (ssNMR) enables detailed bone analysis. This study used multiple-quantum/single-quantum (MQ/SQ) correlation experiments to reveal collagen

Keywords:
1Hbonecollagendipolar couplingfast MASmulti‐quantum NMR

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Area of Science:

  • Biophysics
  • Solid-state Nuclear Magnetic Resonance (ssNMR) Spectroscopy
  • Materials Science

Background:

  • Fast magic angle spinning (MAS) in ssNMR is crucial for high-resolution structural analysis of biological systems.
  • Studying complex biomaterials like native bone using ssNMR has been challenging due to limitations in current techniques.
  • Understanding the structural integrity of collagen in native bone is vital for biomaterial research.

Purpose of the Study:

  • To demonstrate the feasibility of using fast MAS ssNMR with MQ/SQ correlation experiments on native bone.
  • To investigate the 1H-1H dipolar coupling networks within the collagen protein in native bone.
  • To explore the role of these networks in maintaining the stability of the collagen triple helix.

Main Methods:

  • Acquisition of two-dimensional (2D) 1H-1H correlation spectra using multiple-quantum/single-quantum (MQ/SQ) correlation experiments.
  • Application of fast MAS (70 kHz) ssNMR techniques to native bone samples.
  • Analysis of 1H-1H dipolar coupling networks to identify structural features.

Main Results:

  • Successfully acquired 2D 1H-1H correlation spectra for native bone at 70 kHz MAS.
  • Uncovered distinct 1H-1H dipolar coupling networks involving long-chain charged residues of collagen.
  • Highlighted the significant role of these collagen networks in stabilizing the triple helix structure.

Conclusions:

  • Fast MAS ssNMR with MQ/SQ correlation experiments is a feasible and powerful technique for analyzing native bone.
  • The study provides new insights into the structural organization and stability of collagen in native bone.
  • This approach opens new possibilities for 1H-detected multi-quantum ssNMR experiments on collagen-containing biological systems.