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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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Protein Folding01:22

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Overview
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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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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.
The...
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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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通过使用ABACUS-T的多式逆折叠来增强功能性蛋白质.

Yufeng Liu1,2, Rui Wu1,2, Xinyu Wang1,2

  • 1Department of Rheumatology and Immunology, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, Hefei National Research Center for Physical Sciences at the Microscale, Center for Advanced Interdisciplinary Science and Biomedicine of IHM, University of Science and Technology of China, Hefei, Anhui, China.

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概括

新型蛋白质重新设计模型ABACUS-T通过整合原子细节,语言模型和进化数据来增强稳定性和功能. 这种工具最大限度地减少了工程蛋白质的功能损失,显示了结合亲和力和热稳定性的显著改善.

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科学领域:

  • 蛋白质工程是一种蛋白质工程.
  • 计算生物学是一种计算生物学.
  • 生物技术是生物技术.

背景情况:

  • 基于结构的蛋白质重新设计旨在提高稳定性,但往往会降低功能.
  • 现有的反向折叠模型难以平衡稳定性和活动性.
  • 需要先进的模型,将多样化的生物数据纳入精确的蛋白质工程.

研究的目的:

  • 介绍ABACUS-T,这是一个多式联接式反向折叠模型.
  • 提高蛋白质序列重新设计的精度,同时最大限度地减少功能性妥协.
  • 在重新设计的蛋白质中表现出增强的稳定性和保留/改进的功能.

主要方法:

  • 开发了ABACUS-T,集成了原子侧链,配体相互作用,蛋白质语言模型,多个脊柱形状和多个序列对齐 (MSA) 数据.
  • 应用ABACUS-T来重新设计蛋白质,包括一种结蛋白,内-1,4-β-xylanase,TEM β-lactamase和OXA β-lactamase.
  • 评估了重新设计的蛋白质的结合亲和力,形状变化,酶活性,基质选择性和热稳定性.

主要成果:

  • 重新设计的酶结合蛋白显示出17倍更高的亲和力,保留了形状变化.
  • 内分-1,4-β-xylanase和TEMβ-lactamase保持或超过了野生类型的活性.
  • OXAβ-乳糖酶表现出改变的基质选择性.
  • 所有重新设计的蛋白质都显示出显著增加的热稳定性 (∆Tm ≥10°C).
  • 通过少数序列实现了增强,每个序列都含有众多同时发生的突变.

结论:

  • ABACUS-T有效地增强了蛋白质的结构稳定性和功能活性.
  • 该模型的多式联接方法克服了现有的反向折叠方法的局限性.
  • 在生物技术中,ABACUS-T是重新设计功能性蛋白质的有希望的工具.