Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Antibody Structure

Antibody Structure

Antibody Structure

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...

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...

Antibody Structure and Classes

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.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Development of bispecific antibodies with enhanced neutralization activity against tested SARS-CoV-2 Omicron subvariants.

Frontiers in immunology·2026

Same author

Predominant HLA class I associations with lupus nephritis susceptibility, histology class and reduced renal function in patients with systemic lupus erythematosus: a retrospective case-control study.

Rheumatology international·2026

Same author

Increased Risk of Injury in Patients with Fabry Disease: A Nationwide Population-Based Cohort Study in Taiwan.

International journal of medical sciences·2026

Same author

Healthcare utilization and costs in patients with rheumatoid arthritis using biologics or tofacitinib: a nationwide, population-based study.

Clinical rheumatology·2026

Same author

Longitudinal Trajectories and Predictors of Health-Related Quality of Life in Systemic Lupus Erythematosus: A 2-Year Longitudinal Cohort Study.

Rheumatology and therapy·2026

Same author

Genetic polymorphisms associated with therapeutic response and adverse effects to methotrexate in Taiwanese patients with rheumatoid arthritis: a real-world, hospital-based study.

Scientific reports·2026

Same journal

Meet the author: Stephen Brohawn.

Structure (London, England : 1993)·2026

Same journal

Tetraspanins bring Norrin into focus: Structural insights into ligand-specific Wnt signaling.

Structure (London, England : 1993)·2026

Same journal

Uncovering subtype-selective activation of the K<sub>Ca</sub>3.1 channel by SKA-111.

Structure (London, England : 1993)·2026

Same journal

Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.

Structure (London, England : 1993)·2026

Same journal

Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states.

Structure (London, England : 1993)·2026

Same journal

Multifaceted effects of N-glycosylation on amyloidogenic κ light chains in AL amyloidosis.

Structure (London, England : 1993)·2026

See all related articles

Search research articles

Related Experiment Video

Updated: May 5, 2026

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

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

Published on: March 15, 2019

Loop-sequence features and stability determinants in antibody variable domains by high-throughput experiments.

Hung-Ju Chang¹, Jhih-Wei Jian², Hung-Ju Hsu³

¹Genomics Research Center, Academia Sinica, Taipei 115, Taiwan; Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan; Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei 106, Taiwan.

Structure (London, England : 1993)

|November 26, 2013

Summary

This summary is machine-generated.

Protein loops are not the main drivers of antibody function. Instead, distant tertiary interactions dictate protein stability and antigen binding, suggesting loops play a passive role in folding.

More Related Videos

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

VDJ-Seq: Deep Sequencing Analysis of Rearranged Immunoglobulin Heavy Chain Gene to Reveal Clonal Evolution Patterns of B Cell Lymphoma

VDJ-Seq: Deep Sequencing Analysis of Rearranged Immunoglobulin Heavy Chain Gene to Reveal Clonal Evolution Patterns of B Cell Lymphoma

Published on: December 28, 2015

Related Experiment Videos

Last Updated: May 5, 2026

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

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

Published on: March 15, 2019

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

VDJ-Seq: Deep Sequencing Analysis of Rearranged Immunoglobulin Heavy Chain Gene to Reveal Clonal Evolution Patterns of B Cell Lymphoma

VDJ-Seq: Deep Sequencing Analysis of Rearranged Immunoglobulin Heavy Chain Gene to Reveal Clonal Evolution Patterns of B Cell Lymphoma

Published on: December 28, 2015

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Protein loops are crucial for protein structure and function.
High-throughput sequencing and thermal stability measurements advance the study of sequence-structure-function relationships.

Purpose of the Study:

Investigate sequence-structure-function relationships in antibody loops.
Analyze complementarity-determining regions (CDRs) and non-CDR loops in a VEGF-binding scFv.

Main Methods:

Utilized high-throughput DNA sequencing and thermal stability measurements.
Focused on a consensus-sequence optimized single-chain antibody variable fragment (scFv).
Examined six CDRs and ten non-CDR loops in variable domains.

Main Results:

Identified a few key residues with long-range tertiary interactions influencing antigen binding.
Observed that residues distant from the antigen-binding site are critical.
Found limited contribution of local loop sequences to protein stability and function.

Conclusions:

Antibody loops are likely passive in protein folding.
Conserved tertiary interactions primarily dictate essential loop sequences.
Local loop sequence features have minimal impact on protein stability and function.