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Related Concept Videos

Antibody Structure01:10

Antibody Structure

65.6K
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...
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Antibody Structure and Classes01:25

Antibody Structure and Classes

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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.
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Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

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Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
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Structures of Solids02:22

Structures of Solids

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Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
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Antibody Actions01:26

Antibody Actions

2.8K
Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
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Structural Isomerism02:34

Structural Isomerism

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Isomerism in Complexes
Isomers are different chemical species that have the same chemical formula. Structural isomerism of coordination compounds can be divided into two subcategories, the linkage isomers and coordination-sphere isomers.
Linkage isomers occur when the coordination compound contains a ligand that can bind to the transition metal center through two different atoms. For example, the CN− ligand can bind through the carbon atom or through the nitrogen atom. Similarly, SCN− can...
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Related Experiment Video

Updated: Feb 6, 2026

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

Published on: March 15, 2019

13.1K

Structurally Mapping Antibody Repertoires.

Konrad Krawczyk1, Sebastian Kelm2, Aleksandr Kovaltsuk1

  • 1Department of Statistics, Oxford University, Oxford, United Kingdom.

Frontiers in Immunology
|August 8, 2018
PubMed
Summary
This summary is machine-generated.

Analyzing antibody diversity through immunoglobulin gene sequencing (Ig-seq) is now possible. This study successfully mapped millions of antibody sequences to known structures, revealing significant overlap in antibody repertoires.

Keywords:
B-cell receptorantibody specificitybioinformatics toolsnext-generation sequencingproteinstructural homology

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Related Experiment Videos

Last Updated: Feb 6, 2026

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

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Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals
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T and B Cell Receptor Immune Repertoire Analysis using Next-generation Sequencing
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T and B Cell Receptor Immune Repertoire Analysis using Next-generation Sequencing

Published on: January 12, 2021

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Area of Science:

  • Immunology
  • Bioinformatics
  • Structural Biology

Background:

  • The human antibody repertoire exhibits vast theoretical diversity.
  • Next-generation sequencing of immunoglobulin genes (Ig-seq) provides large-scale sequence data of B-cell receptors.
  • Integrating structural information can enhance the analysis of antibody features like binding sites and specificity.

Purpose of the Study:

  • To develop and validate a computational pipeline for structural annotation of antibodies.
  • To map large Ig-seq datasets to known antibody structures.
  • To assess the extent to which diverse antibody sequences can be linked to existing structural data.

Main Methods:

  • Development of a structural annotation pipeline for antibody sequences.
  • Application of the pipeline to five Ig-seq datasets.
  • Analysis of approximately 35 million unique amino acid sequences from 600 individuals.

Main Results:

  • The pipeline successfully mapped a majority of antibody sequences from large Ig-seq datasets to known structures.
  • Demonstrated the feasibility of structural annotation across diverse datasets and individuals.
  • Confirmed that despite theoretical diversity, many antibody sequences share structural similarities.

Conclusions:

  • Structural annotation of antibody sequences derived from Ig-seq is a viable approach.
  • This method enriches sequence data with crucial structural and functional insights.
  • The findings suggest a degree of convergence in antibody structural space across individuals.