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

NMR Spectrometers: Overview01:20

NMR Spectrometers: Overview

1.0K
NMR spectrometers consist of a strong magnet, a radiofrequency transmitter, and a detector attached to a computer console for recording spectra of samples containing NMR-active nuclei. In first-generation NMR instruments called continuous-wave spectrometers, the resonance frequencies of the nuclei are determined by frequency-sweep or field-sweep methods. The magnetic field strength is fixed and the rf signal is swept in the former, while the radiofrequency signal is fixed and the magnetic field...
1.0K
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

658
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...
658
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.0K
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...
1.0K
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

166
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...
166
NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

1.2K
The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...
1.2K
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

599
In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
599

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

Protonated Structure of EmrE Reveals C-terminal Tail Gating Mechanism.

bioRxiv : the preprint server for biology·2026
Same author

Probing Solution Dynamics of Tissue Factor Using Molecular Dynamics Simulations Guided by NMR Chemical Shifts.

The journal of physical chemistry. B·2026
Same author

<i>In vitro</i>-prepared A30P alpha-synuclein fibrils adopt the conserved and disease-relevant Greek key fold.

bioRxiv : the preprint server for biology·2026
Same author

Top-Down Scoring of Spectral Fitness by Image Analysis for Protein Structure Validation.

Journal of chemical information and modeling·2025
Same author

NMR Spectral Alignment Utilizing a CryoEM Motion Correction Algorithm.

Analytical chemistry·2025
Same author

Backbone assignment of a 28.5 kDa class A extended spectrum β-lactamase by high-field, carbon-detected solid-state NMR.

Biomolecular NMR assignments·2025
Same journal

Linker Engineering toward NIR-II Metal-Organic Framework with Maximal Emission beyond 1000 nm for Inflammatory Bowel Disease Imaging.

Journal of the American Chemical Society·2026
Same journal

Observing Kinetic Selectivity in Anthracene Photodimerization through Selective Quenching by Excited States of Proximate Rare Earth Cations.

Journal of the American Chemical Society·2026
Same journal

Sequence-Dependent Folding of Recognition-Encoded Melamine Oligomers.

Journal of the American Chemical Society·2026
Same journal

Large Thermo- and Mechanosalient Actuation via Cooperative Twist Elasticity-Induced Packing Motif Conversion.

Journal of the American Chemical Society·2026
Same journal

Discovery and Biosynthesis of Lanthipeptides Featuring an Azepinoindole Scaffold by Radical <i>S</i>-Adenosylmethionine Enzyme-Catalyzed C-C Bond Formation.

Journal of the American Chemical Society·2026
Same journal

Enantiopurity-Controlled Magnetism in a Two-Dimensional Organic-Inorganic Material.

Journal of the American Chemical Society·2026
関連記事をすべて見る

関連する実験動画

Updated: Jun 2, 2025

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode
09:19

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode

Published on: June 4, 2021

3.2K

OPTO: 固体NMRスペクトロシーの自動最適化

Collin G Borcik1,2, Barry DeZonia1,2, Thirupathi Ravula1,2

  • 1Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.

Journal of the American Chemical Society
|January 15, 2025
PubMed
まとめ
この要約は機械生成です。

OPTOソフトウェアは,パラメータ最適化を自動化することで,固体NMR (SSNMR) 実験を簡素化します. これは複雑な生物学的および物質的なシステムを研究する研究者のデータ品質とアクセシビリティを向上させます.

さらに関連する動画

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

5.1K
NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements
08:54

NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements

Published on: May 1, 2017

26.0K

関連する実験動画

Last Updated: Jun 2, 2025

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode
09:19

NMR-Based Fragment Screening in a Minimum Sample but Maximum Automation Mode

Published on: June 4, 2021

3.2K
15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

5.1K
NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements
08:54

NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements

Published on: May 1, 2017

26.0K

科学分野:

  • 固体核磁共振 (SSNMR) スペクトロシー
  • 生物物理化学
  • 材料科学

背景:

  • SSNMRは生物学的および物質的なシステムにユニークな洞察を提供します.
  • 複雑な多次元パルス配列は,大きなバイオ分子でのサイト解析測定に不可欠です.
  • 複製可能な高品質のSSNMRデータを得ることは,広範なユーザートレーニングと難しいパラメータ最適化のために困難です.

研究 の 目的:

  • SSNMRの課題を克服するために設計されたソフトウェアオペレーティング環境であるOPTOを紹介します.
  • 一般的に使用されるSSNMR実験の性能とアクセシビリティを向上させる.
  • 実験条件の信頼性の高い最適化とデータ品質の改善を可能にします.

主な方法:

  • OPTOの開発,グラフィカルユーザーインターフェースのソフトウェア環境.
  • 自動パラメータチューニングのための最適化アルゴリズム (シンプレックス,グリッド検索) の統合.
  • Varian OpenVnmrJ と Bruker Topspin のソフトウェアプラットフォームとの互換性
  • シャミング,クロスポラライゼーション,その他の実験パラメータの自動化最適化の実証.

主要な成果:

  • 解像度を向上させるため,21の輝くパラメータの自動化されたグローバル検索を通じて, 100億分の12のライン幅を達成しました.
  • 双極化条件の16のパラメータを最適化することで,トリプル共振実験の感度が向上した.
  • タンパク質サンプルを用いた複数のスペクトロメーター,磁場強度,魔法の角度回転率における結果の堅実性と再現性を実証した.

結論:

  • OPTOのソフトウェアは,SSNMRのデータ取得と分析におけるボトルネックを効果的に解決します.
  • ソフトウェアは,機器の時間を活用し,オペレータが最適な実験条件を確実に見つけられるようにします.
  • OPTOは,高品質で再現可能なSSNMRデータの生成を促進し,生物分子構造,動力学,および機能の研究を進めています.