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相关概念视频

Hemoglobin01:24

Hemoglobin

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Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
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Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...
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Cooperative Allosteric Transitions01:58

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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...
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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy
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血红蛋白功能的可预测收具有不可预测的分子基础

Chandrasekhar Natarajan1, Federico G Hoffmann2, Roy E Weber3

  • 1School of Biological Sciences, University of Nebraska, Lincoln, NE 68588, USA.

Science (New York, N.Y.)
|November 16, 2016
PubMed
概括
此摘要是机器生成的。

基因适应显示出可预测的功能变化, 但不可预测的分子根源. 历史突变和遗传背景限制了进化途径,这意味着适应性解决方案在物种中并不普遍.

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科学领域:

  • 进化生物学
  • 分子进化
  • 生物化学

背景情况:

  • 基因适应驱动着进化变化.
  • 血红蛋白与氧气的亲和力对于高海拔生存至关重要.
  • 了解融合揭示了进化的可预测性.

研究的目的:

  • 研究遗传适应的可预测性.
  • 检查融合血红蛋白功能演化的分子基础.
  • 评估历史意外性在适应中的作用.

主要方法:

  • 具有不同海拔范围的56种鸟类类的比较分析.
  • 在血红蛋白中进行氨基酸替代分析.
  • 实验使用复活的祖先蛋白质.

主要成果:

  • 在高海拔鸟类中,血红蛋白与氧气亲和度的趋同增加是常见的.
  • 由于并行氨基酸的替代,很少出现融合的功能变化.
  • 历史上的替代对蛋白质功能有上下文依赖的影响.
  • 遗传背景影响了突变的适应潜力.

结论:

  • 生物化学表型可以显示可预测的适应性.
  • 适应的分子基础并不总是可以预测的.
  • 进化适应受到历史偶然性和遗传背景的限制.