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相关概念视频

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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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:
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Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

107
Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
107
Complexometric Titration: Ligands00:43

Complexometric Titration: Ligands

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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...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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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...
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相关实验视频

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Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
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确定营养物质的干-传感器结合亲和力.

Xin Gu1,2,3

  • 1Department of Neurobiology, Harvard Medical School, Boston, MA, USA. xin_gu@hms.harvard.edu.

Methods in molecular biology (Clifton, N.J.)
|February 24, 2025
PubMed
概括

一个新的协议量化了营养传感器结合亲和力,这对于理解细胞生长调节至关重要. 该方法使用S-adenosylmethionine和SAMTOR,确定营养感应机制是否具有生理相关性.

关键词:
亲密关系珠子的珠子具有竞争力的具有约束力的分析.营养传感器的营养传感器营养素 营养素 营养素蛋白质净化 蛋白质的净化放射性联结体是一种放射性联结体.这是一种闪的闪.在 mTORC1 的情况下,mTORC1 是

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相关实验视频

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科学领域:

  • 细胞生物学 细胞生物学
  • 生物化学 生物化学
  • 代谢过程中的代谢.

背景情况:

  • 细胞拥有传感生长调节环境营养的机制.
  • 机械性目标的拉帕米辛复合物1 (mTORC1) 集成的生长因素和营养物质,如氨基酸.
  • 营养传感器结合连接体来信号营养的可用性,并调节mTORC1信号.

研究的目的:

  • 开发一种可靠的方法来定量确定营养素的传感器-连接物结合亲和力 (Kd).
  • 通过比较结合亲和力与生理代谢物范围来评估营养感应机制的生理相关性.
  • 提供一个可通用的协议,用于可重复的营养物联体-营养物传感器结合亲和力的确定.

主要方法:

  • 营养传感器 (SAMTOR) 的净化.
  • 用放射性营养物联体 (S-adenosylmethionine) 进行化.
  • 闪计数和结合亲和力 (Kd) 的数学计算.

主要成果:

  • 该协议允许可重复确定营养物质传感器结合亲和力.
  • 定量代谢分析提供了代谢产物的生理范围.
  • 将结合亲和力与生理范围的比较表明了传感机制的相关性.

结论:

  • 描述的协议允许定量评估营养物质传感器-连接体结合亲和力.
  • 这种方法对于了解细胞如何根据营养的可用性调节生长是必不可少的.
  • S-adenosylmethionine-SAMTOR对作为这种可通用技术的模型.