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Related Concept Videos

2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

910
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...
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2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

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

1.6K
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...
1.6K
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.7K
Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
1.7K
NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

11.8K
In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
11.8K
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

805
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...
805
Proton (¹H) NMR: Chemical Shift01:07

Proton (¹H) NMR: Chemical Shift

4.3K
Organic molecules primarily contain carbon and hydrogen atoms. While all the hydrogen isotopes are NMR-active, protium or hydrogen-1 is the most abundant. It has a significant energy separation between its nuclear spin states due to its large gyromagnetic ratio. As per Boltzmann's distribution, an increase in the energy separation implies a greater excess population of nuclei available for excitation, resulting in a strong NMR absorption signal.
Absorption signals of all the protium nuclei...
4.3K

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Related Experiment Video

Updated: Apr 7, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
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High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

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High Pressure NMR Spectroscopy.

Kazuyuki Akasaka1

  • 1High Pressure Protein Research Center, Institute of Advanced Technology, Kinki University, 930 Nishimitani, Kinokawa, 649-6493, Japan, akasaka@kpu.ac.jp.

Sub-Cellular Biochemistry
|July 16, 2015
PubMed
Summary

High pressure NMR spectroscopy reveals that proteins universally contain high-energy substates. This technique allows systematic analysis of protein structures and thermodynamic stability, previously undetectable.

Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • High-energy substates in proteins are crucial for function but difficult to study.
  • Conventional spectroscopic methods, including NMR, typically cannot detect low-population substates.

Purpose of the Study:

  • To introduce high pressure NMR spectroscopy as a method for detecting and analyzing protein high-energy substates.
  • To demonstrate the universal presence and thermodynamic stability of these substates.

Main Methods:

  • Variable-pressure NMR spectroscopy (high pressure NMR spectroscopy) was employed.
  • This technique uses pressure perturbation to amplify and detect subtle structural changes.

Main Results:

  • High pressure NMR spectroscopy unequivocally confirmed the universal presence of high-energy conformers in proteins.

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High-Sensitivity Nuclear Magnetic Resonance at Giga-Pascal Pressures: A New Tool for Probing Electronic and Chemical Properties of Condensed Matter under Extreme Conditions
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High-Sensitivity Nuclear Magnetic Resonance at Giga-Pascal Pressures: A New Tool for Probing Electronic and Chemical Properties of Condensed Matter under Extreme Conditions

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High-Temperature and High-Pressure In situ Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy
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Related Experiment Videos

Last Updated: Apr 7, 2026

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High-Sensitivity Nuclear Magnetic Resonance at Giga-Pascal Pressures: A New Tool for Probing Electronic and Chemical Properties of Condensed Matter under Extreme Conditions
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  • These substates exist in equilibrium with stable folded states.

    • Conclusions:

    • High pressure NMR spectroscopy provides a systematic approach to studying protein intrinsic fluctuations.
    • The technique is valuable for understanding protein structure, stability, and dynamics, with potential for other biomacromolecules.