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相关概念视频

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Structural Protein Function01:56

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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Blood clotting or coagulation involves extrinsic and intrinsic pathways, which ultimately merge into the common pathway, forming a fibrin clot.
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相关实验视频

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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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由内在无序的部分产生的力调整蛋白质功能

Nicholas D Keul1, Krishnadev Oruganty2, Elizabeth T Schaper Bergman3

  • 1Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA.

Nature
|November 14, 2018
PubMed
概括

本质上无序的片可以通过转移形态组合来增强蛋白质功能. 这种由无序区域的长度驱动的热效应优化了UDP-α-D-葡萄糖-6-脱酶 (UGDH) 的抑制剂结合.

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科学领域:

  • 生物化学
  • 结构生物学
  • 进化生物学

背景情况:

  • 蛋白质结构是动态的,探索各种对功能至关重要的结构.
  • 蛋白质进化和功能中的内在无序区域的作用尚不清楚.
  • 人类蛋白质组的很大一部分含有未知功能的内在无序部分.

研究的目的:

  • 调查内在无序的片如何影响蛋白质构成和功能.
  • 确定本质上失序的碳酸终端影响蛋白质 - 连接体相互作用的机制.
  • 在蛋白质适应过程中探索内在无序部分的进化含义.

主要方法:

  • 研究了人类的UDP-α-D-葡萄糖-6-脱酶 (UGDH) 蛋白质.
  • 研究了内在无序的碳酸终端尾 (ID-尾) 对UGDH的形状组合的影响.
  • 分析了ID尾部长度与异质抑制剂的亲和关系.

主要成果:

  • ID尾部将UGDH形态组合转移到一种对全抑制剂的更高亲和度的状态.
  • 观察到的亲和度增强取决于内在无序段的长度,而不是其序列或组成.
  • 这种效应与非结构化产生的力一致.

结论:

  • 本质上是无序的尾巴作为一个"直器",通过调节蛋白质动态和结构来促进抑制剂的结合.
  • 这种机制提供了易于获得的适应性,表明进化可能会选择无序的部分来调整蛋白质能量格局.
  • 这些发现为蛋白质组内在疾病的流行提供了潜在的解释.