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相关概念视频

Antibody Structure01:10

Antibody Structure

58.6K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
58.6K
Protein Folding01:25

Protein Folding

7.6K
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...
7.6K
Antibody Structure and Classes01:25

Antibody Structure and Classes

703
Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
703
Protein Organization01:24

Protein Organization

6.0K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
6.0K
Immunoprecipitation01:20

Immunoprecipitation

5.1K
Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
5.1K

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相关实验视频

Updated: May 16, 2025

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments
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Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

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抗折叠:使用反向折叠改进了基于结构的抗体设计.

Magnus Haraldson Høie1, Alissa M Hummer2, Tobias H Olsen2

  • 1Section for Bioinformatics, Department of Health Technology, Technical University of Denmark, Lyngby DK-2800, Denmark.

Bioinformatics advances
|April 2, 2025
PubMed
概括

新的抗体特异逆折叠模型AntiFold通过保持结构完整性来增强抗体设计. 它改善了序列恢复,并预测了抗原结合亲和力,有助于抗体优化.

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

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相关实验视频

Last Updated: May 16, 2025

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Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

Published on: October 15, 2016

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

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科学领域:

  • * 计算生物学 计算生物学
  • * 蛋白质工程是指蛋白质的工程.
  • * 免疫学 免疫学

背景情况:

  • * 抗体设计和优化需要平衡多种属性.
  • * 蛋白质逆折叠模型为单个结构生成多种序列,保持结构完整性.
  • * 现有的反向折叠工具在抗体特定应用方面存在局限性.

研究的目的:

  • * 推出AntiFold,一种针对抗体的反向折叠模型.
  • * 评估AntiFold在序列恢复和结构相似性的性能.
  • * 评估AntiFold在预测抗体-抗原结合亲缘关系方面的能力.

主要方法:

  • *对ESM-IF1模型在已解决和预测的抗体结构上进行微调.
  • * 在互补性确定区域 (CDR) 中评估序列恢复.
  • *评估设计和解决的抗体结构之间的结构相似性.
  • *对抗体-抗原结合亲和力的零射击预测.

主要成果:

  • * AntiFold 在跨CDR的序列恢复方面超过了现有的反向折叠工具.
  • * 设计的序列与其已解决的对应物具有很高的结构相似性.
  • *AntiFold在预测抗体-抗原结合亲和力方面表现出更强的相关性.
  • * 该模型将破坏抗原结合的突变赋予低概率.

结论:

  • *AntiFold是抗体设计和优化的一个有前途的工具.
  • * 它有效地保持结构完整性,同时改善序列恢复.
  • * 该模型有助于预测和指导抗体-抗原结合亲和力.
  • *AntiFold与蛋白质语言模型协同,用于增强抗体工程.