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相关概念视频

Phosphodiester Linkages01:01

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Overview
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...
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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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The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
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相关实验视频

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Measuring Proliferation of Vascular Smooth Muscle Cells Using Click Chemistry
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点击链接:基于点击化学的细胞兼容蛋白质交叉链接方法.

Bruno C Amaral1, Andrew R M Michael1, Nicholas I Brodie1

  • 1Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, AL, Canada.

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概括

这项研究引入了一种新的交叉连接策略,以显著提高使用交叉连接质谱法 (XL-MS) 绘制人类互动原子的深度. 新方法实现了检测到的蛋白质-蛋白质相互作用 (PPI) 的20倍增加,超过了现有技术.

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科学领域:

  • 蛋白质组学是指蛋白质组学.
  • 生物化学 生物化学
  • 分子生物学分子生物学

背景情况:

  • 交联质谱 (XL-MS) 是绘制蛋白质-蛋白质相互作用 (PPI) 的一个强大的技术.
  • 目前的XL-MS方法的采样深度很低,这限制了它们对互动组进行全面分析的能力.
  • 现有的方法,如亲和力拉向MS是间接的,容易出错.

研究的目的:

  • 开发一种先进的交叉连接策略,以克服XL-MS的低采样深度限制.
  • 显著增加可检测的蛋白质-蛋白质相互作用 (PPI) 的数量,以实现高分辨率的互动组映射.
  • 为了更准确,更全面地了解空间蛋白质组.

主要方法:

  • 开发了一种由两个步骤组成的顺序和直角交叉连接策略.
  • 该方法涉及使用免疫光启发的固定协议预先稳定空间蛋白质组.
  • 表面可访问的氨酸被标记为N-氧苏胺 (N-hydroxysuccinimide,NHS) 修饰的点击试剂,然后用铜催化的化-化循环添加 (CuAAC) 来进行交叉连接.

主要成果:

  • 新的交叉连接策略实现了接近总信号30%的交叉连接水平.
  • 检测到蛋白与蛋白相互作用 (PPI) 的水平大约是传统 DSS 方法的 20 倍.
  • 该方法表明没有可检测的副作用或空间蛋白质组的扭曲.

结论:

  • 开发的交叉连接策略大大提高了XL-MS的采样深度.
  • 这种方法比现有的绘制人类互动组图的技术有了显著的改进.
  • 该方法提供了高保真,高分辨率的蛋白质-蛋白质相互作用的绘制,前所未有的深度.