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関連する概念動画

NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.0K
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...
3.0K
Structures of Solids02:22

Structures of Solids

17.5K
Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
17.5K
NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

11.0K
In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
11.0K
NMR Spectroscopy of Aromatic Compounds01:14

NMR Spectroscopy of Aromatic Compounds

6.2K
Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
6.2K
NMR Spectroscopy of Benzene Derivatives01:34

NMR Spectroscopy of Benzene Derivatives

11.1K
Simple unsubstituted benzene has six aromatic protons, all chemically equivalent. Therefore, benzene exhibits only a singlet peak at δ 7.3 ppm in the 1H NMR spectrum. The observed shift is far downfield because the aromatic ring current strongly deshields the protons. Any substitution on the benzene ring makes the aromatic protons nonequivalent, and the protons split each other. The peak is, therefore, no longer a singlet and the splitting pattern and their associated coupling...
11.1K
Protein and Protein Structure02:15

Protein and Protein Structure

87.0K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
87.0K

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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

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13Cスピン拡散固体NMR光譜によるタンパク質構造の決定.

Theofanis Manolikas1, Torsten Herrmann, Beat H Meier

  • 1Physical Chemistry, ETH Zurich, CH-8093 Zurich, Switzerland.

Journal of the American Chemical Society
|March 7, 2008
PubMed
まとめ
この要約は機械生成です。

プロトン駆動13Cスピン拡散 (PDSD) NMRは,原子解像度でタンパク質構造を決定する. この強固な方法は,マイクロ結晶のサンプルにおけるクロスピーク強度からの核間距離情報を使用しています.

さらに関連する動画

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

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

Published on: December 16, 2013

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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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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
  • 核磁共振スペクトロスコピー 核磁共振スペクトロスコピー

背景:

  • プロトン駆動13Cスピン拡散 (PDSD) は2D NMR技術である.
  • PDSDは,原子核間の距離情報を持つ高い信号から騒音のスペクトルを生成します.

研究 の 目的:

  • PDSDを用いた原子解像度タンパク質構造の決定を実証する.
  • 交差ピークの強度と核間距離の関係を調査する.

主な方法:

  • 均一に13C,15Nとラベル付けされたマイクロクリスタリンタンパク質サンプル (ユビキチン) を使用しました.
  • 手動で構造を決定し,その後に自動化された最適化を採用した.
  • 完全に自動化された構造決定アプローチを適用しました.

主要な成果:

  • ユビキチンの原子解像度構造の決定を達成しました.
  • 構造分析のためのPDSD情報コンテンツの十分性を示しました.
  • スペクトルクロスピーク強度と核間距離の相関を調査した.

結論:

  • PDSDは,タンパク質構造の解明のための強力で汎用的なNMR実験です.
  • この方法は,単一のマイクロ結晶のサンプルから構造の決定を可能にします.
  • 距離-強度相関のさらなる理解は,構造分析を洗練することができます.