Diversity of Amino Acids in Antibodies
Jason Huang
Antibody Variations
AP Biology
EO1
Explain how variations within a class of molecules allows for a greater diversity of functions. Focus on antibody variations.
During an immune response, the white blood cells including T cells and B cells bind to the antigen. Antigens are chemicals released from invading pathogens or toxins. The binding of antigen to the antigen receptors of T cells or B cells help activate and secrete antibodies to bind to the antigen receptor protein on the membrane of a pathogen. The binding of antibodies to a specific receptor of pathogen activates the resistance.
When a B cell recognizes an antigen, the B cell has antigen receptors with 2 heavy chains and two identical chains joined by disulfide bonds. This gives a Y shape fore each antigen receptor protein on a B cell. An antigen receptor protein consists of two sites: a constant region (C) and a variable (V) region. In the constant region, the amino acid sequences remain similar to another antigen receptor from another B cell. What determines the main difference in targeting specific types pathogen for each B cell is the variable region. A variable region of an antigen receptor from one B cell has completely different amino acid sequencing than the variable region of another antigen receptor from another B cell. Thus, the variable region forms a bond with the specific antigen. This in terms activates the B cell to secrete antibodies. Similar to the Y-shaped structure of the antigen receptor, antibodies target on specific antigen binding site on a pathogen. Such process inactivates the infections from pathogen. After all, the variable region of an antigen receptor of a B cell provides a diverse variety of combinations of amino acids. This allows a greater diversity of specializing each B cell to target on specific pathogen.
Unlike the B cell, T cell has antigen receptors that bind to the specific parts of antigens. A T cell antigen receptor also consists of a
Antibody Variations
AP Biology
EO1
Explain how variations within a class of molecules allows for a greater diversity of functions. Focus on antibody variations.
During an immune response, the white blood cells including T cells and B cells bind to the antigen. Antigens are chemicals released from invading pathogens or toxins. The binding of antigen to the antigen receptors of T cells or B cells help activate and secrete antibodies to bind to the antigen receptor protein on the membrane of a pathogen. The binding of antibodies to a specific receptor of pathogen activates the resistance.
When a B cell recognizes an antigen, the B cell has antigen receptors with 2 heavy chains and two identical chains joined by disulfide bonds. This gives a Y shape fore each antigen receptor protein on a B cell. An antigen receptor protein consists of two sites: a constant region (C) and a variable (V) region. In the constant region, the amino acid sequences remain similar to another antigen receptor from another B cell. What determines the main difference in targeting specific types pathogen for each B cell is the variable region. A variable region of an antigen receptor from one B cell has completely different amino acid sequencing than the variable region of another antigen receptor from another B cell. Thus, the variable region forms a bond with the specific antigen. This in terms activates the B cell to secrete antibodies. Similar to the Y-shaped structure of the antigen receptor, antibodies target on specific antigen binding site on a pathogen. Such process inactivates the infections from pathogen. After all, the variable region of an antigen receptor of a B cell provides a diverse variety of combinations of amino acids. This allows a greater diversity of specializing each B cell to target on specific pathogen.
Unlike the B cell, T cell has antigen receptors that bind to the specific parts of antigens. A T cell antigen receptor also consists of a