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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.

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...

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Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
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Related Experiment Video

Updated: Jun 27, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Published on: September 12, 2019

Characterizing antibody specificity to different protein morphologies by AFM.

Min S Wang¹, Andleeb Zameer, Sharareh Emadi

¹Department of Chemical Engineering, Arizona State University, Tempe, Arizona 85287-6006, USA.

Langmuir : the ACS Journal of Surfaces and Colloids

|December 19, 2008

Summary

Atomic force microscopy (AFM) characterized alpha-synuclein (alphaS) binding with antibody fragments. This technique can distinguish between different alphaS aggregate morphologies, aiding in neurodegenerative disease diagnostics.

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Area of Science:

Neuroscience
Biochemistry
Immunology

Background:

Protein misfolding and aggregation are implicated in neurodegenerative diseases like Alzheimer's, Parkinson's, and Huntington's.
Aggregated proteins share a common cross beta-sheet conformation, but their specific roles in disease are debated.
Distinguishing between different protein aggregate morphologies in situ is crucial for understanding disease mechanisms.

Purpose of the Study:

To characterize the binding of single chain antibody fragments (scFvs) to different alpha-synuclein (alphaS) morphologies using atomic force microscopy (AFM).
To evaluate the potential of scFvs as diagnostic tools for protein misfolding diseases.

Main Methods:

Utilized atomic force microscopy (AFM) to analyze topographic images of alpha-synuclein (alphaS) aggregates.
Characterized the binding specificity of three different single chain antibody fragments (scFvs) to various alphaS morphologies.
Compared height distributions of alphaS aggregates with and without scFv addition to determine binding patterns.

Main Results:

One scFv demonstrated binding to all tested alphaS morphologies.
A second scFv selectively bound to oligomeric alphaS.
A third scFv specifically recognized fibrillar alphaS.

Conclusions:

AFM is a versatile and accessible technique for characterizing antigen-antibody interactions.
The developed scFvs show potential as immunodiagnostics for differentiating protein aggregate morphologies in neurodegenerative diseases.