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Complexometric Titration: Ligands00:43

Complexometric Titration: Ligands

2.5K
Different monodentate and polydentate ligands are used as complexing agents in complexometric titration reactions. The formation of complexes by mono- and bidentate ligands involves two or more intermediate steps, limiting their use as complexing agents. In comparison, polydentate ligands can form complexes with metal ions in a single-step process, facilitating sharper end points. This means polydentate ligands, such as amino carboxylic acid derivatives, are most commonly employed in...
2.5K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.2K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.2K
Extraction: Advanced Methods00:56

Extraction: Advanced Methods

1.3K
Metal ions can be separated from one another by complexation with organic ligands–the chelating agent– to form uncharged chelates. Here, the chelating agent must contain hydrophobic groups and behave as a weak acid, losing a proton to bind with the metal. Since most organic ligands used in this process are insoluble or undergo oxidation in the aqueous phase, the chelating agent is initially added to the organic phase and extracted into the aqueous phase. The metal-ligand complex is...
1.3K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

4.4K
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...
4.4K
Formation of Complex Ions03:45

Formation of Complex Ions

18.8K
A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...
18.8K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

10.6K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
10.6K

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関連する実験動画

Updated: May 5, 2026

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

Published on: April 5, 2022

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Cu ((I)) の生化学に対する堅固な親和基準.

Pritha Bagchi1, M Thomas Morgan, John Bacsa

  • 1School of Chemistry and Biochemistry, Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology , 901 Atlantic Drive, Atlanta, Georgia 30332, United States.

Journal of the American Chemical Society
|December 5, 2013
PubMed
まとめ
この要約は機械生成です。

研究者は,銅とタンパク質の結合親和性を正確に測定するために,新しい銅 (I) リガンド (MCL) を開発しました. これらの安定リガンドは,銅の相互作用を定量化するための信頼できる基準を提供し,生物学的プロセスを理解するために不可欠です.

さらに関連する動画

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

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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
09:14

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Published on: July 20, 2016

39.3K

関連する実験動画

Last Updated: May 5, 2026

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

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

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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
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Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Published on: July 20, 2016

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科学分野:

  • バイオケミストリー バイオケミストリー
  • 無機化学 無機化学とは
  • メタロタンパク質化学 メタロタンパク質化学

背景:

  • 銅の精確な測定は,信頼性の高い参照リガンドの欠如によって阻害されています.
  • 参照リガンドに関する既存の文献は稀で,しばしば矛盾しており,実験的解釈を複雑にしています.

研究 の 目的:

  • Cu ((I)) 結合親和度測定のための新しい水溶性単価銅リガンド (MCLs) を開発し,特徴づけること.
  • 水溶液中のCu (I) 複合化に対する信頼性の高い親和度基準のセットを確立する.
  • 既存のリファレンスのリガンドを新しいMCLシリーズと比較して校正する.

主な方法:

  • 3つの単価銅リガンド (MCL-1,MCL-2,MCL-3) の合成と特徴付け.
  • X線結晶学,電気化学分析,均衡定位実験により,複雑な構造と安定定数を決定する.
  • バトクープロインジスルフォネートと2,2'-ビシンコニン酸の安定常数に対するMCLシリーズに対する校正.

主要な成果:

  • MCL-1,MCL-2,MCL-3は,水中の1:1ステキオメトリーを持つ,はっきりと定義された,空気に安定した,無色のCu (III) 複合体を形成する.
  • これらのリガンドは,広範囲 (10−10から10−17M) のCu (I) 濃度をバッファリングする.
  • CusFのCu(I) 結合親和性は,log K = 14.3 ± 0.1として決定され,MCLシリーズの有用性を実証しました.

結論:

  • 開発されたMCLシリーズは,正確なCu (I) 結合親近性決定のための堅牢で信頼性の高い基盤を提供します.
  • これらのリンガンドは,タンパク質および小分子とのCu (I) 相互作用の正確な定量化を促進します.
  • この研究は,銅とタンパク質の相互作用を研究する方法論の重要なギャップに対処しています.