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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: 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...
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...
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...
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.

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Related Experiment Video

Updated: Jun 21, 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 3D sidechain correlation in solid-state proteins.

Ye Tian1, Lingling Chen, Dimitri Niks

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

Physical Chemistry Chemical Physics : PCCP
|August 5, 2009
PubMed
Summary
This summary is machine-generated.

New 3D experiments enable detailed carbon-13 (13C) sidechain correlation in solid-state proteins. These methods provide high-quality spectra for protein assignment, even for large enzymes.

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Last Updated: Jun 21, 2026

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

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Published on: September 17, 2017

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
11:22

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions

Published on: January 30, 2018

Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Solid-state NMR is crucial for determining protein structures.
  • Carbon-13 (13C) based experiments are vital for protein resonance assignment.
  • Challenges remain in obtaining high-resolution spectra for large proteins.

Purpose of the Study:

  • To develop novel 3D scalar-based homonuclear correlation experiments for solid-state proteins.
  • To improve spectral resolution and band selectivity for 13C sidechain correlation.
  • To facilitate the assignment of spectra for both small and large solid-state proteins.

Main Methods:

  • Development and application of sensitive constant-time 3D homonuclear correlation experiments.
  • Utilizing scalar couplings for polarization transfer, decoupled during chemical shift evolution.
  • Demonstration of pulse sequences for sidechain-to-backbone carbonyl and purely sidechain correlations.

Main Results:

  • High-quality spectra with unique sidechain correlations achieved for small proteins (e.g., GB1) at 9.4 Tesla.
  • Demonstrated polarization transfer efficiency of approximately 30% over two bonds.
  • Successful application to a large enzyme (tryptophan synthase, 140 kDa) at 400 MHz, with well-resolved 2D spectra at 900 MHz.

Conclusions:

  • The developed methods provide essential 13C-13C correlations for protein assignment in the solid state.
  • These techniques offer optimism for assigning spectra of large enzymes, overcoming previous limitations.
  • The approach is effective for both small proteins and large, complex enzyme systems.