Antibodies Flashcards
What type of proteins are antibodies
Globular glycoproteins called immunoglobulins
Describe the structure of antibodies
Antibodies have a quaternary structure, presented as a Y shape, with 2 ‘heavy’ (long) polypeptide chains bonded by disulfide bonds to 2 ‘light’ (short) polypeptide chains.
What two regions does each polypeptide chain have
a constant region and a variable reason
Do the constant regions vary
They do not vary within a class (isotope) of antibodies but do vary between the classes.
What does the constant region do
Determines the mechanism used to destroy the antigens
What is the amino acid sequence in the variable regions of antibodies like for each antibody
each antibodies variable region is made up of a different amino acid sequence
What happens at the variable region in the antibody
where the antibody attaches to the antigen to form an antigen - antibody complex
What is at the end of the variable region
The antigen - binding site
how many amino acids is in each antigen-binding site
110-130 different amino acids
How does the antibody get its specificity for binding
The antigen - binding sites vary greatly
What is the epitope
part of the antigen that binds to antibody
What does the ‘hinge’ region allow the antibody to do
gives flexibility to the antibody which allows different angles when binding to antigens
is the ‘hinge’ region present in all classes of antibodies
No
What do antigens and their complimentary antibody have
Complementary molecule molecular shapes
What happens if an antibody randomly collides with a foreign cell that possesses non-self antigens antigens with a complementary shape
it binds with an antigen to form an antigen-antibody complex