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

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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

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

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...
Atomic Nuclei: Nuclear Relaxation Processes01:23

Atomic Nuclei: Nuclear Relaxation Processes

In the absence of an external magnetic field, nuclear spin states are degenerate and randomly oriented. When a magnetic field is applied, the spins begin to precess and orient themselves along (lower energy) or against (higher energy) the direction of the field. At equilibrium, a slight excess population of spins exists in the lower energy state. Because the direction of the magnetic field is fixed as the z-axis,  the precessing magnetic moments are randomly oriented around the z-axis. This...
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...
Atomic Nuclei: Types of Nuclear Relaxation01:28

Atomic Nuclei: Types of Nuclear Relaxation

Nuclear relaxation restores the equilibrium population imbalance and can occur via spin–lattice or spin–spin mechanisms, which are first-order exponential decay processes.
In spin–lattice or longitudinal relaxation, the excited spins exchange energy with the surrounding lattice as they return to the lower energy level. Among several mechanisms that contribute to spin–lattice relaxation, magnetic dipolar interactions are significant. Here, the excited nucleus transfers energy to a nearby...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...

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関連する実験動画

Updated: Jul 1, 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

マッピングポリペプチドの自己認識は, (1) Hオフ共振のリラックスによる.

Veronica Esposito1, Rahul Das, Giuseppe Melacini

  • 1Departments of Chemistry, Biochemistry and Biomedical Sciences, McMaster University, 1280 Main Street W., Hamilton, Ontario L8S 4M1, Canada.

Journal of the American Chemical Society
|June 30, 2005
PubMed
まとめ

この研究は,アミロイド線維生成における弱い相互作用を正確にマッピングするための新しい核磁気共鳴 (NMR) 方法を導入しています. この技術は実験的な課題を克服し,アミロイド原性ペプチドとタンパク質-リガンドの相互作用の研究を助けます.

科学分野:

  • 生物物理化学 生物物理化学
  • 構造生物学 構造生物学とは
  • 神経科学は神経科学である.

背景:

  • 核磁共鳴 (NMR) のリラクゼーション速度は,弱い分子相互作用に敏感であり,アミロイド線維生成におけるポリペプチドオリゴメリゼーションを理解するために重要である.
  • リラクゼーション率を測定する従来のNMR方法は,J移転と選択性の問題を含む実験的な課題に直面しており,初期段階のアミロイド形成の研究を妨げています.
  • 神経退行性疾患に関与するアミロイド線維生は,特徴づけが難しい複雑なポリペプチド相互作用を伴う.

研究 の 目的:

  • 弱い相互作用のリラックス率の測定における実験的限界を克服するために,新しいNMRベースのアプローチを開発し,検証する.
  • この方法をアミロイドベータ (Abeta) (12-28) ペプチドの自己認識相互作用をマッピングするために適用する.
  • アミロイド原性ペプチドとタンパク質-リガンドの相互作用を研究するための技術の広範な適用性を実証する.

主な方法:

  • 35.5度傾いた有効フィールドを使用して非選択的オフ共振1Hリラックス速度を測定.
  • Carr-Purcell-Meiboom-Gill (CPMG) と逆転回復実験に固有のJ移転と選択性の問題を回避する.
  • アベタ (12-28) ペプチドのハルファスピンに適用して,残留分辨率マップを生成する.

主要な成果:

さらに関連する動画

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

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: Jul 1, 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

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

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

  • 提案されたNMR実験は,従来のリラクゼーション速度測定に関連する実験的課題を効果的に回避しています.
  • アベタ (12-28) ペプチドの残留解像度自己認識マップが生成されました.
  • 取得したマップは,独立した変異研究の結果と一致しており,その方法の正確性を検証しています.

結論:

  • 新しいNMR技術は,ポリペプチドオリゴメリゼーションにおける弱い相互作用を調査するための堅牢で敏感な方法を提供します.
  • このアプローチは,アミロイドフィブリロゲネシスの初期段階を研究し,アミロイド生成ペプチドの特徴を定めるのに非常に価値があります.
  • この方法は,タンパク質-リガンド相互作用のスクリーニングとマッピングに広く適用可能であり,薬剤発見と構造生物学において重要な可能性を秘めています.