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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.
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...
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...
¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
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...
Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the others.

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
09:25

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins

Published on: November 1, 2024

Heteronuclear proton assisted recoupling.

Gaël De Paëpe1, Józef R Lewandowski, Antoine Loquet

  • 1Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA. gael.depaepe@cea.fr

The Journal of Chemical Physics
|March 10, 2011
PubMed
Summary
This summary is machine-generated.

We developed a new method, proton assisted insensitive nuclei cross polarization (PAIN-CP), to detect long-distance (15)N-(13)C contacts in biomolecules. This technique enhances structural studies of proteins by revealing intramolecular and intermolecular interactions.

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Area of Science:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy
  • Biomolecular structural biology
  • Advanced pulse sequence development

Background:

  • Detecting long-range nuclear spin-spin interactions is crucial for biomolecular structure determination.
  • Existing methods for (15)N-(13)C cross-polarization can be limited by dipolar truncation and require specific experimental conditions.

Purpose of the Study:

  • To present a theoretical framework and experimental validation of a novel heteronuclear polarization transfer mechanism.
  • To demonstrate the utility of proton assisted insensitive nuclei cross polarization (PAIN-CP) for detecting long-distance (15)N-(13)C contacts in proteins.

Main Methods:

  • Development of the PAIN-CP pulse sequence based on average Hamiltonian theory.
  • Derivation of effective Hamiltonians describing zero- and double-quantum (15)N-(13)C recoupling mediated by proton-nuclear couplings.
  • Analytical and numerical simulations to optimize PAIN-CP parameters and understand its dependence on molecular geometry.
  • Acquisition of solid-state (15)N-(13)C NMR spectra of microcrystalline GB1 and Crh proteins at high magnetic fields and spinning frequencies.

Main Results:

  • PAIN-CP effectively mediates zero- and double-quantum (15)N-(13)C recoupling through trilinear spin interactions.
  • Optimization maps and matching conditions for PAIN-CP were elucidated, showing reduced dipolar truncation.
  • Long-distance intramonomer and intermonomer (15)N-(13)C contacts were successfully detected in GB1 and Crh proteins.
  • The obtained distance restraints were used for structural calculations of the Crh protein monomer.

Conclusions:

  • PAIN-CP is a powerful technique for mapping long-range (15)N-(13)C interactions in solid biomolecules.
  • The method offers advantages in overcoming dipolar truncation, enabling more comprehensive structural analysis.
  • PAIN-CP significantly contributes to the structural characterization of proteins and other biomolecular systems.