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Nuclear Magnetic Resonance (NMR): Overview01:07

Nuclear Magnetic Resonance (NMR): Overview

Nuclear magnetic resonance (NMR) is a phenomenon exhibited by certain nuclei that can absorb characteristic radio frequency radiation under certain conditions. NMR has been extensively applied in molecular spectroscopy and medical diagnostic imaging. In both these applications, the molecule or subject under study is placed in a magnetic field and irradiated with radio frequency energy.
NMR spectroscopy generates a spectrum where the characteristic absorption frequencies of the sample are...
Proton (¹H) NMR: Chemical Shift01:07

Proton (¹H) NMR: Chemical Shift

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 in a...
¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

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 first.
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.
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
The...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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関連する実験動画

Updated: Jun 30, 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

細胞内のタンパク質の特徴づけと割り当てのための多次元NMRスペクトロスコーピー.

Patrick N Reardon1, Leonard D Spicer

  • 1Departments of Biochemistry and Radiology, Duke University Medical Center, Durham, NC 27710, USA.

Journal of the American Chemical Society
|August 4, 2005
PubMed
まとめ

この研究では,生体細胞内のタンパク質を分析するための高速3D核磁気共振 (NMR) 実験を紹介しています. これらの急速な技術により,Escherichia coliのGB-1タンパク質の完全な骨幹配分が可能になり,以前の制限を克服しました.

科学分野:

  • バイオ物理化学 バイオ物理化学
  • 構造生物学 構造生物学とは
  • 分子生物物理学 分子生物物理学

背景:

  • 高フィールド,ヘテロ核核磁気共振 (NMR) スペクトロスコピーは,生物学的マクロ分子の研究に不可欠です.
  • タンパク質を本来の細胞環境内で分析することは,低濃度と長い実験時間のために困難です.
  • タンパク質の特徴づけのための従来の3DNMR実験は,in vivoアプリケーションにはしばしば時間がかかりすぎて,細胞の生存能力を制限します.

研究 の 目的:

  • 生物学的マクロ分子 in vivo の分析のための高速 3D NMR 実験のスイートを開発し,実装する.
  • 細胞NMR研究における長いデータ取得時間の限界を克服するために.
  • 生きたEscherichia coli細胞内の再結合タンパク質の完全なバックボーン割り当てを達成するために.

主な方法:

  • 冷たい探査機による高フィールド (600MHz) ヘテロ核性NMRスペクトロスコーピーを利用しました.
  • 迅速なデータ取得のために投影再構築技術を採用した.
  • (3,2) HNCA, (3,2) HNCO,および (3,2) HA(CA) NH.を含む,3D NMR実験を高速に実施しました.

主要な成果:

  • 迅速な3D NMR実験を in vivoで成功裏に実施しました.

さらに関連する動画

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

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

関連する実験動画

Last Updated: Jun 30, 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

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

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

  • 再結合ポリペプチド GB-1 の共鳴の完全なバックボーン割り当てを生成しました.
  • 生きた細菌の細胞内のタンパク質から詳細な構造情報を得ることの実現可能性を示した.

    • 結論:

    • 急速な3D NMR技術により,タンパク質の原生細胞文脈におけるタンパク質の in vivo 構造の研究が効率的に可能になります.
    • このアプローチは,以前の時間制約を克服し,生存可能な細胞内のタンパク質の詳細な特徴づけを可能にします.
    • 開発された方法は,複雑な生物学的システムの高度なセルラーNMR調査の道を開く.