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

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.3K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.3K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.4K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
8.4K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

6.3K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.3K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

8.7K
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
8.7K
Colors and Magnetism03:02

Colors and Magnetism

13.1K
Color in Coordination Complexes
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human...
13.1K

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

Tracking the Early Hydration Reaction of Cementitious Calcium Silicate Hydrate via DNP-Enhanced Solid-State NMR.

Journal of the American Chemical Society·2026
Same author

Mapping mRNA Localization and Internal Structure in Lipid Nanoparticles through Solid-State Dynamic Nuclear Polarization NMR and Proton Spin-Diffusion Modeling.

Small methods·2026
Same author

A Rigid Supramolecular Solution to a Flexible Problem: A Multifunctional Calix[4]arene-Based Strategy to Prevent α‑Synuclein Toxicity.

ACS central science·2026
Same author

Electronic Structures of Pt(0) Complexes and Atomically Precise Clusters from Solid-State <sup>195</sup>Pt NMR Signatures.

Journal of the American Chemical Society·2026
Same author

In Situ Light-Induced Degradation of Hybrid Perovskites by NMR Spectroscopy.

Journal of the American Chemical Society·2026
Same author

Fluorinated Biradicals for <sup>19</sup>F Magic-Angle Spinning Dynamic Nuclear Polarization-Enhanced NMR Spectroscopy.

Journal of the American Chemical Society·2026

関連する実験動画

Updated: Dec 1, 2025

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

9.6K

スーパーオキシードディスミュータゼダイナミクスにおける銅結合に対する多様式反応

Marta Bonaccorsi1, Michael J Knight1, Tanguy Le Marchand1

  • 1Centre de RMN à Très Hauts Champs, FRE 2034 (CNRS/Université Claude Bernard Lyon 1/Ecole Normale Supérieure de Lyon), University of Lyon, 69100 Villeurbanne, France.

Journal of the American Chemical Society
|November 9, 2020
PubMed
まとめ

銅/亜鉛超酸化変異酵素 (SOD) の動態は,2つの金属化形態で研究された. 金属イオンの吸収は タンパク質の柔軟性を調整し 様々な時間スケールでの動きに影響します

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

9.9K
Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
11:38

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

2.8K

関連する実験動画

Last Updated: Dec 1, 2025

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

9.6K
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

9.9K
Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores
11:38

Quantifying the Binding Interactions Between CuII and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

2.8K

科学分野:

  • 生物化学
  • バイオ物理学
  • 構造生物学

背景:

  • 銅/亜鉛超酸化変異酵素 (SOD) は,アミオトロフィック横筋硬化症に関与する重要な金属酵素である.
  • SODの構造と機能の関係を理解することは,神経変性疾患の研究に不可欠です.

研究 の 目的:

  • SODのダイナミクスに対するメタレーションの影響を調査する.
  • SODの異なる金属化状態でのタンパク質の動きを定量化する.

主な方法:

  • 固体核磁気共振 (NMR) スペクトロスコーピー
  • 高磁場 (800-1000MHz) で高速なマジック・アングル・スピニング (MAS)
  • Cu,Zn-SODとE,Zn-SODのマイクロ結晶製剤の分析

主要な成果:

  • 金属イオン吸収はSODを硬化させないが,運動プロセスを再分配する.
  • 動きはナノ秒からミリ秒までのダイナミック範囲で定量化されました
  • ヒスティジンのサイドチェーンダイナミクスと遠隔のバックボーン要素の結合が観察されました.

結論:

  • 金属化状態はSODのダイナミックな風景に大きな影響を与えます.
  • SODの柔軟性は金属イオンの組み込みによって微調整され,タンパク質の機能に影響します.
  • これらの発見は,病気のメカニズムにおけるSODの役割についての洞察を提供します.