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Related Concept Videos

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: 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: 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...
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

The coupling interactions of nuclei across four or more bonds are usually weak, with J values less than 1 Hz. While these are usually not observed in spectra, the presence of multiple bonds along the coupling pathway can result in observable long-range coupling.
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene π orbitals.
Insensitive Nuclei Enhanced by Polarization Transfer (INEPT)01:15

Insensitive Nuclei Enhanced by Polarization Transfer (INEPT)

Insensitive Nuclei Enhanced by Polarization Transfer (INEPT) is an advanced Nuclear Magnetic Resonance (NMR) technique specifically designed to detect and enhance the signals of low-abundance nuclei, such as carbon-13 and nitrogen-15, in small molecules. The fundamental principle behind INEPT is the transfer of polarization from a more abundant and highly polarizable nucleus, typically hydrogen-1, to the low-abundance nucleus of interest. This process effectively boosts the NMR signal of the...

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Cortical Actin Flow in T Cells Quantified by Spatio-temporal Image Correlation Spectroscopy of Structured Illumination Microscopy Data
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High-resolution local field spectroscopy with internuclear correlations.

Alexander A Nevzorov1

  • 1Department of Chemistry, North Carolina State University, Raleigh, NC 27695-8204, USA. alex_nevzorov@ncsu.edu

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|September 8, 2009
PubMed
Summary
This summary is machine-generated.

This study introduces a new pulse sequence for solid-state NMR, improving spectral assignment and revealing contacts in membrane proteins. It enhances structural analysis by reducing spectral crowding for better protein studies.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Correlating distant spins (>3Å) is challenging in solid-state NMR for oriented membrane proteins.
  • Accurate spectral assignment and understanding interhelical contacts are crucial for structural elucidation.

Purpose of the Study:

  • To present a novel pulse sequence for solid-state NMR of oriented membrane proteins.
  • To overcome limitations in spectral assignment and the determination of interhelical contacts.

Main Methods:

  • Incorporation of mismatched Hartmann-Hahn mixing of dilute spins via a proton bath.
  • Utilization of high-resolution local field spectroscopy.
  • Employing dipolar couplings in the indirect dimension for spectral analysis.

Main Results:

  • The new pulse sequence effectively establishes correlations among distant spins.
  • It significantly reduces spectral crowdedness compared to standard homonuclear correlation techniques.
  • Provides valuable structural information and aids in spectral assignment.

Conclusions:

  • The proposed pulse sequence is a valuable tool for spectral assignment in solid-state NMR.
  • It facilitates the elucidation of interhelical contacts in uniaxially oriented membrane proteins.
  • Enhances structural studies of membrane proteins using NMR.