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Antigen-induced conformational changes in antibodies: a problem for structural prediction and design
1Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.
Recent work has shown that large conformational changes in antibodies can accompany antigen binding. These structural changes can alter dramatically the size, shape and charge distribution in the antigen-binding pocket, and may present problems for accurate modeling of antibody structures.
Recent work has shown that large conformational changes in antibodies can accompany antigen binding. These structural changes can alter dramatically the size, shape and charge distribution in the antigen-binding pocket, and may present problems for accurate modeling of antibody structures.
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Antibody Structure
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.
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Antibody Structure
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.
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Antibodies consist of four polypeptide chains: two identical heavy...
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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.
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Antibodies can bind to pathogens, preventing them from infecting host cells. This process...