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Related Concept Videos

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...
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...
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.
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

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...
Protein Folding01:22

Protein Folding

Overview

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Related Experiment Video

Updated: Jun 17, 2026

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments
12:28

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

Published on: October 15, 2016

How antibodies fold.

Matthias J Feige1, Linda M Hendershot, Johannes Buchner

  • 1Center for Integrated Protein Science, Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany.

Trends in Biochemical Sciences
|December 22, 2009
PubMed
Summary

B cells employ unique DNA strategies to produce antibodies, necessitating robust quality control. This study reveals how diverse immunoglobulin folding mechanisms ensure protein accuracy during B cell transport.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • B cells generate a vast antibody repertoire from limited DNA, increasing the risk of protein misfolding.
  • Antibody production relies on cellular quality control (QC) to ensure protein function and prevent cellular stress.

Purpose of the Study:

  • To elucidate the diverse folding strategies of immunoglobulin (Ig) domains.
  • To understand how these folding properties are integrated into cellular checkpoints for Ig transport and quality assurance.

Main Methods:

  • In vitro experiments characterizing Ig domain folding.
  • In vivo studies examining the role of folding in cellular Ig transport and quality control.

Main Results:

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Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
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Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy

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Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments
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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

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  • Ig domains exhibit varied folding strategies, from spontaneous self-folding to partner-dependent folding.
  • Distinct folding characteristics correlate with specific cellular checkpoints governing Ig trafficking.
  • B cells actively monitor and regulate Ig protein folding and assembly.

    • Conclusions:

    • The diverse folding mechanisms of Ig domains are critical for B cell antibody production.
    • Cellular checkpoints effectively monitor Ig folding and assembly, ensuring the fidelity of antibody proteins.
    • Understanding these QC mechanisms provides insights into B cell biology and potential therapeutic targets.