The antigen-binding sites of an antibody molecule are formed from the molecule's variable regions which are described as so because their amino acid sequences can be different on different antibodies.
The specificity of antibodies is determined by the variable regions found at their endpoints. Antibodies are specialized proteins secreted by B-cells of the immune system. They are also called immunoglobulins. They contain four polypeptide chains that comprise two heavy chains and two light chains to form a Y-shaped molecule.
The variable regions, more specifically the hypervariable regions of an antibody, have a high ratio of different amino acids with the most common amino acids provided in one place. The variable region serves as the antigen-binding site while the constant region found below the variable region is determined to invade the antigen.
Antibodies are preserved in our body to identify the antigen the next time it encounters. They send the signals to the other body parts to reject the antigen and invade it.
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If the adjacent angles of a parallelogram measure 25° and 155°, the other two angles would measure 25° and 155°
<h3>What is a
parallelogram?</h3>
A parallelogram is a quadrilateral (has four sides and four angles) in which both sides are equal and parallel to each other. Opposite angles of a parallelogram have the same measure and the diagonals are equal in length.
If the adjacent angles of a parallelogram measure 25° and 155°, the other two angles would measure 25° and 155° because opposite angles are equal.
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