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

¹H NMR: Interpreting Distorted and Overlapping Signals

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 slanted or...
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.
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
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...

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Updated: Jul 7, 2026

Multimodal Nonlinear Hyperspectral Chemical Imaging Using Line-Scanning Vibrational Sum-Frequency Generation Microscopy
08:49

Multimodal Nonlinear Hyperspectral Chemical Imaging Using Line-Scanning Vibrational Sum-Frequency Generation Microscopy

Published on: December 1, 2023

非線形サンプリングによる超次元NMRスペクトロスコーピー.

Victor A Jaravine1, Anastasia V Zhuravleva, Perttu Permi

  • 1Swedish NMR Centre, Göteborg University, Box 465, 40530 Göteborg, Sweden.

Journal of the American Chemical Society
|March 4, 2008
PubMed
まとめ

この研究は,核磁共鳴 (NMR) データ分析のための新しい方法を導入し,収集時間を100倍大幅に短縮します. この進歩により,構造生物学におけるタンパク質構造の迅速で自動化された決定が可能になります.

科学分野:

  • 構造生物学 構造生物学とは
  • バイオフィジックス 生物物理学
  • アナリティカル・ケミストリー (Analytical Chemistry) とは

背景:

  • 核磁共振 (NMR) スペクトロスコピーは,タンパク質の構造を決定する上で極めて重要です.
  • 従来のNMRデータ取得と分析は時間がかかり,高通量アプリケーションを制限しています.
  • 現在の方法は,スペクトルの複雑さや大量のデータセットで苦労しています.

研究 の 目的:

  • 共同インターリーブ記録,リアルタイム処理,およびNMRデータの分析のための効率的なアプローチを開発する.
  • スペクトルの解像度と感度を維持しながら,データ収集時間を大幅に短縮します.
  • 自動分析を可能にし,タンパク質構造の決定を加速します.

主な方法:

  • 非線形サンプリングモードで記録されたトリプル共振スペクトルの多次元分解を使用します.
  • 従来のスペクトルからハイパー次元 (HD) スペクトルモデルを構築します.
  • タンパク質システムの自動割り当て戦略を利用します.

主要な成果:

  • NMRデータ収集時間を平均2桁 (100倍) 短縮する.
  • リアルタイムでデータを収集し,ユビキチン (8 kDa) を約1時間で,ゼタサイト (13 kDa) を約10時間でバックボーン割り当てを行う.

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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

関連する実験動画

Last Updated: Jul 7, 2026

Multimodal Nonlinear Hyperspectral Chemical Imaging Using Line-Scanning Vibrational Sum-Frequency Generation Microscopy
08:49

Multimodal Nonlinear Hyperspectral Chemical Imaging Using Line-Scanning Vibrational Sum-Frequency Generation Microscopy

Published on: December 1, 2023

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)
10:28

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

  • 自然に乱れたものを含む,異なる複雑さのタンパク質の自動割り当てを実証します.

    • 結論:

    • 開発されたアプローチは,NMRデータ取得と分析における重要な時間的なボトルネックを排除します.
    • ハイパー次元 (HD) のスペクトルは,簡単に処理され,自動分析が可能である.
    • 構造生物学,特に高通量構造ゲノミクスのためのNMRスペクトロスコピーの価値を大幅に高めます.