Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

801
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...
801
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

992
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
992
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.3K
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...
1.3K
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

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

1.3K
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...
1.3K
¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

1.7K
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...
1.7K
¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

1.7K
A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied...
1.7K

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

The NMR Exchange Format (NEF): Specification and Applications.

bioRxiv : the preprint server for biology·2026
Same author

Antibacterial Drug Discovery: Deep Learning Successes and Challenges through the Structural Biology Lens.

Computational and structural biotechnology journal·2026
Same author

Structural determinants of endopilus assembly, stability and functional specificity in bacterial type II secretion.

bioRxiv : the preprint server for biology·2026
Same author

AI-Enhanced Adaptive Virtual Screening Platform Enabling Exploration of 69 Billion Molecules Discovers Structurally Validated FSP1 Inhibitors.

bioRxiv : the preprint server for biology·2026
Same author

Colouring dysbiosis: FetB-dependent Mn-PPIX produced by Porphyromonas gingivalis shapes the oral microbiota.

NPJ biofilms and microbiomes·2026
Same author

Corrections to "Discovery of the Cytocapsular Membrane as Hallmark of Malignant Tumors".

Biochemistry·2026

関連する実験動画

Updated: Apr 27, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

16.8K

断面的に補償された,稀に非均一なサンプリングされた4Dプロトン-プロトン拘束装置から固体NMR構造の決定.

Rasmus Linser1, Benjamin Bardiaux, Loren B Andreas

  • 1Max-Planck Institute for Biophysical Chemistry , Am Fassberg 11, 37077 Göttingen, Germany.

Journal of the American Chemical Society
|July 3, 2014
PubMed
まとめ

この研究では,精密なタンパク質構造の決定のために,対角抑制と非均一なサンプリング (NUS) を使用した新しい固体NMR法が導入されています. このテクニックはスペクトルの明晰さを高め,タンパク質構造を計算するための信頼性の高い制約を生成します.

さらに関連する動画

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

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

Published on: December 16, 2013

9.3K
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

2.0K

関連する実験動画

Last Updated: Apr 27, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

16.8K
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

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

Published on: December 16, 2013

9.3K
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

2.0K

科学分野:

  • バイオフィジックス 生物物理学
  • 構造生物学 構造生物学とは
  • 核磁共振 (NMR) スペクトロスコピー

背景:

  • 固体NMRはタンパク質構造の決定に不可欠ですが,スペクトルの解釈は困難です.
  • NMRスペクトルの強力な自己相関信号 (対角ピーク) は,しばしば重要な交差ピークを遮り,正確な構造分析を妨げます.
  • 既存の方法は,スペクトルの重複とダイナミックレンジの制限に苦しんでおり,構造的な制約の質に影響を与えています.

研究 の 目的:

  • 縦断的に補償されたタンパク質構造的制約を取得するための新しい4次元の固体NMRアプローチを開発し,検証する.
  • 明確なスペクトル解釈を可能にすることで,構造計算の正確性と信頼性を向上させる.
  • この方法の適用性を,マイクロ結晶やアミロイド繊維を含む多様なタンパク質システムに実証する.

主な方法:

  • 4次元固体NMRにおける対角抑制による同核陽子対陽子相関を用いた.
  • 2%のサンプリング密度で非均一なサンプリング (NUS) を採用し,信号の強度が高い時間領域領域に焦点を当てています.
  • 大幅にデュテラ化され,陽子逆交換されたタンパク質サンプルにこの方法を適用した.

主要な成果:

  • 以前は対角信号によって遮られ,または重複によってバイアスされていたクロスピークの正確な識別を達成しました.
  • 曖昧なスペクトル解釈と,構造計算のための信頼できる構造的制約のセットを生成しました.
  • 非対角抑制スペクトルと比較して,SH3マイクロクリスタルの構造アンサンブル品質の改善が実証されました.
  • 部分的に割り当てられたヒドロフォビン棒の重要なクロスピークの識別が可能になり,構造的解明が容易になりました.

結論:

  • 4D固体NMRにおける診断抑制は,高品質のタンパク質構造的制約を得るための効果的な戦略です.
  • 縦断抑制とNUSの組み合わせは,複雑なタンパク質システムの構造研究のための堅牢で効率的なアプローチを提供します.
  • この方法は,スペクトルの明晰さと信頼性を大幅に高め,構造生物学分野を前進させます.