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

2D NMR: Overview of Heteronuclear Correlation Techniques

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 axis.
2D NMR: Homonuclear Correlation Spectroscopy (COSY)01:06

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

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...
2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

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

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...
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.
¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons01:03

¹H NMR Chemical Shift Equivalence: Homotopic and Heterotopic Protons

Protons in identical electronic environments within a molecule are chemically equivalent and have the same chemical shift. The replacement test is a useful tool to identify chemical equivalence and predict NMR spectra. A substituent replaces each of the protons being examined and the resulting molecules are compared. If the same molecule is obtained, the protons are equivalent or homotopic. Replacement of any hydrogens in ethane by chlorine yields chloroethane because all six protons are...

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Related Experiment Video

Updated: Jul 8, 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

J-based 2D homonuclear and heteronuclear correlation in solid-state proteins.

Lingling Chen1, J Michael Kaiser, Jinfeng Lai

  • 1Department of Chemistry, University of California, Riverside, California 92521, USA.

Magnetic Resonance in Chemistry : MRC
|December 25, 2007
PubMed
Summary
This summary is machine-generated.

New solid-state nuclear magnetic resonance (NMR) experiments enable precise chemical shift correlation for NCO and NCA, aiding protein resonance assignment. These methods enhance spectral resolution without sacrificing sensitivity, proving valuable for complex biomolecules.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

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Last Updated: Jul 8, 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

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) Spectroscopy
  • Biomolecular Structure Determination
  • Protein Resonance Assignment

Background:

  • Solid-state NMR is crucial for studying protein structures and dynamics, particularly for insoluble or aggregated proteins.
  • Accurate assignment of backbone resonances is essential for interpreting solid-state NMR spectra and determining protein structure.
  • Traditional methods can face challenges with spectral resolution and sensitivity in complex protein systems.

Purpose of the Study:

  • To develop and validate novel scalar-based 2D heteronuclear NMR experiments for NCO and NCA chemical shift correlation in the solid state.
  • To demonstrate the utility of these experiments, combined with homonuclear CACO correlation, for tracing connectivities and assigning backbone resonances in solid-state proteins.
  • To assess the performance of these experiments under various magnetic field strengths, decoupling conditions, and magic-angle spinning (MAS) frequencies.

Main Methods:

  • Implementation of scalar-based, constant-time J-based 2D heteronuclear NCO and NCA correlation experiments.
  • Application of these experiments to two model proteins: the beta 1 immunoglobulin binding domain of protein G and reassembled thioredoxin.
  • Utilized different magnetic field strengths (9.4 T and 14.1 T), decoupling techniques, and MAS frequencies.
  • Explored compatibility with in-phase anti-phase (IPAP) selection for enhanced resolution.

Main Results:

  • Successful demonstration of NCO and NCA chemical shift correlation in the solid state, facilitating backbone resonance assignment.
  • Enhanced spectral resolution in the indirect dimension achieved through effective homonuclear and heteronuclear decoupling.
  • Constant-time nature of the experiments preserved sensitivity while improving resolution, avoiding a common trade-off.
  • Compatibility with IPAP selection further improved resolution in the directly detected dimension.

Conclusions:

  • The developed scalar-based 2D heteronuclear experiments provide a powerful and sensitive toolkit for solid-state protein resonance assignment.
  • These methods offer improved spectral resolution, crucial for analyzing complex biological systems using solid-state NMR.
  • The demonstrated applicability across different experimental conditions highlights the robustness and versatility of this approach.