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Related Concept Videos

Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
Antibody Structure and Classes01:25

Antibody Structure and Classes

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.
Antibody Structure01:10

Antibody Structure

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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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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 form...

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Updated: Jun 15, 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

Maximum entropy models for antibody diversity.

Thierry Mora1, Aleksandra M Walczak, William Bialek

  • 1Joseph Henry Laboratories of Physics and Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544, USA.

Proceedings of the National Academy of Sciences of the United States of America
|March 10, 2010
PubMed
Summary
This summary is machine-generated.

Maximum entropy models reveal that zebrafish IgM sequences exhibit restricted diversity due to correlations, not independent mutations. This suggests antibody diversity is shaped by adaptation, not just genomic limits.

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13:14

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

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Area of Science:

  • Immunology
  • Computational Biology
  • Protein Sequence Analysis

Background:

  • Pathogen recognition depends on diverse protein families, including antibodies.
  • Understanding the statistical properties of antibody repertoires is crucial for immunology.
  • Previous models often assumed independent amino acid substitutions, potentially oversimplifying diversity.

Purpose of the Study:

  • To construct and validate maximum entropy models for zebrafish IgM sequence repertoires.
  • To investigate the statistical properties and diversity constraints of antibody sequences.
  • To explore the implications of sequence correlations for antibody evolution and adaptation.

Main Methods:

  • Developed maximum entropy models based on pairwise residue correlations from experimental IgM sequence data.
  • Interpreted models using statistical physics principles to predict repertoire properties.
  • Compared model predictions with experimental data and contrasted with independent substitution models.

Main Results:

  • Models accurately captured higher-order statistical properties of the IgM repertoire.
  • Predicted sequence distribution follows Zipf's law, with repertoire clustering and massive diversity restriction due to correlations.
  • Findings contradicted models assuming independent amino acid substitutions and aligned well with empirical data.

Conclusions:

  • Antibody diversity is significantly constrained by correlations between residue positions, not solely by genomic encoding.
  • Observed diversity patterns suggest rapid adaptation to antigenic challenges plays a key role in antibody evolution.
  • The maximum entropy modeling approach is broadly applicable to studying global properties of other protein families.