Functions Of The Different Types Of Antibodies And How Their Structure

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Immunoglobulins (Ig) are proteins that are utilized by the immune system to recognize and destroy foreign entities such as viruses and bacteria. They are created by a type of white blood cell called plasma cells. Immunoglobulins, also known as antibodies, recognize special indicators on the entities which are called antigens. When the immune system recognizes a foreign substance in the body, it sends antibodies to attack them. Antigens have specific structures that are recognized by certain antibodies and therefore each antibody is specifically created to only attack one specific type of antigen. This research paper will outline the structure and functions of the different types of antibodies and will describe how their structure relates to function. Structure: Every antibody is composed of four polypeptides; two light chains and two heavy chains. These chains form together to make a “Y” shaped molecule with the heavy chains on the inside making the general shape and the light chains on the top outer edge of the protein. The light chain is composed of approximately 214 amino acids and the heavy chain is composed of about twice as many amino acids. There is also a vast amount of amino acid sequences at the ends of the protein that makes each one different from the others. The top end of the antibody is known as the variable region, composed of approximately 110-130 amino acids, and is what gives antibodies their specificity and uniqueness for binding to certain antigens
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