The Immune System: Antibody Structure

These flashcards cover key concepts related to the structure and functions of antibodies as discussed in the lecture.

Antibody

A protein produced by B cells that binds to specific antigens to neutralize them.

Immunoglobulin G (IgG)

A type of antibody molecule that is composed of two identical light chains and two identical heavy chains.

Fab region

Fragment antigen binding region of an antibody that binds to the antigen.

Fc region

Fragment crystallizable region of an antibody that mediates effector functions.

Variable region

Region of an antibody that shows high variability in amino acid sequence, determining antigen specificity.

Constant region

Region of an antibody with limited sequence variation.

Hinge region

Flexible region of an antibody that allows movement between the Fab and Fc regions.

Hypervariable regions (HVs)

Discrete loops in the V domains of antibodies that contribute to high variability in binding affinity to antigens.

Epitope

The specific part of an antigen that is recognized and bound by an antibody.

Affinity

The strength of the binding interaction between an antibody and a single antigen epitope.

Avidity

The overall strength of binding between an antibody and an antigen, considering multiple binding sites.

ELISA (Enzyme Linked Immunosorbent Assay)

A laboratory technique used to detect and quantify proteins, such as antibodies, in a sample.

Western blot

A technique used to detect specific proteins in a sample through gel electrophoresis followed by transfer to a membrane.