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相关概念视频

Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Two structural features of the DNA molecule provide a basis for the mechanisms of heredity: the four nucleotide bases and its double-stranded nature. The Watson-Crick model of double-helical DNA structure, proposed in 1952, drew heavily upon the X-ray crystallography work of researchers Rosalind Franklin and Maurice Wilkins. Watson, Crick, and Wilkins jointly received the Nobel Prize in Physiology or Medicine for their work in 1962. Franklin was, controversially, excluded from the prize for...
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Deoxyribonucleic acid, or DNA, is the genetic material responsible for passing traits from generation to generation in all organisms and most viruses. DNA is composed of two strands of nucleotides that wind around each other to form a spring-like structure called a double helix. However, the double helix is not perfectly symmetrical. Instead, there are regularly occurring grooves in the structure. The major groove occurs where the sugar-phosphate backbones are relatively far apart. This space...
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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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固态相变作为基因组折叠悖论的解决方案

Joan Pulupa1,2, Natalie G McArthur3, Olga Stathi2

  • 1Department of Biochemistry and Molecular Biophysics, Vagelos College of Physicians and Surgeons, New York, NY, USA.

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概括

神经元中的长距离基因组联系形成了稳定,选择性的增强器枢纽. 这些中心是固态的生物分子凝聚物,由DNA序列和蛋白质相互作用驱动,解释基因组结构.

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科学领域:

  • 分子生物学
  • 基因组学
  • 细胞生物学

背景情况:

  • 超长距离的基因组接触对于神经元基因组结构至关重要,
  • 调节性DNA元素在像嗅觉受体基因调节这样的过程中选择性地接触到远处的序列.

研究的目的:

  • 调查选择性,远程基因组接触的基础上的生物化学机制.
  • 了解嗅觉受体 (OR) 增强器枢纽如何组装和维持它们的结构.

主要方法:

  • 在实验室中使用重组蛋白和DNA组装OR增强器枢纽.
  • 无细胞复制试验以分析凝结物的特性.
  • 在嗅觉神经元 (OSN) 中进行单分子追踪和脉冲追踪实验.

主要成果:

  • 在体外,OR增强剂形成具有固体特性的核蛋白凝聚物.
  • 在OR增强剂中的特定DNA基因协调了凝聚物组合.
  • 在OSN核中,LHX2和EBF1蛋白形成具有固体特性的转录能力的凝聚物.

结论:

  • 同性核蛋白相互作用,受DNA序列的影响,产生新的生物分子凝聚物.
  • 这些固体凝聚物为长距离基因组接触的稳定性和特异性提供了潜在的解释.
  • 这些发现为不同细胞类型的基因组组织提供了可概括的模型.