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Related Concept Videos

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
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...
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.
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...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
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...

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Related Experiment Video

Updated: Jun 6, 2026

Polarization-Sensitive Two-Photon Microscopy for a Label-Free Amyloid Structural Characterization
05:54

Polarization-Sensitive Two-Photon Microscopy for a Label-Free Amyloid Structural Characterization

Published on: September 8, 2023

Polarization-angle-scanning two-dimensional spectroscopy: application to dipeptide structure determination.

Jun-Ho Choi1, Minhaeng Cho

  • 1Department of Chemistry and Research Institute for Natural Sciences, Korea University, Seoul 136-701, Korea.

The Journal of Physical Chemistry. A
|November 18, 2010
PubMed
Summary
This summary is machine-generated.

Polarization-angle-scanning two-dimensional spectroscopy selectively suppresses spectral peaks. This technique aids in determining molecular structures by analyzing transition dipole vectors, offering insights into complex molecular arrangements.

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

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

Published on: December 16, 2013

Area of Science:

  • Physical Chemistry
  • Spectroscopy
  • Molecular Biophysics

Background:

  • Coherent two-dimensional optical spectroscopy utilizes four ultrashort pulses with controllable parameters.
  • Pulse delay times, wavevectors, frequencies, and polarization directions are key experimental variables.

Purpose of the Study:

  • To demonstrate the utility of polarization-angle-scanning two-dimensional spectroscopy for selectively suppressing spectral peaks.
  • To establish theoretical relationships for controlling peak suppression based on transition dipole vectors.
  • To apply this technique for molecular structure determination.

Main Methods:

  • Heterodyne-detected stimulated photon echo measurement.
  • Polarization-angle-scanning two-dimensional spectroscopy.
  • Analysis of amide I vibrations in isotope-labeled dipeptide conformers.

Main Results:

  • Selective suppression of diagonal peaks or cross-peaks in two-dimensional spectra is achievable.
  • Theoretical framework established for vanishing cross-peaks by controlling polarization angles.
  • Demonstrated selective cross-peak suppression in dipeptide conformers.

Conclusions:

  • Polarization-controlled two-dimensional spectroscopy provides detailed molecular structural information.
  • The technique enables determination of relative transition dipole vector orientations.
  • This method serves as a constraint for elucidating peptide structures.