Instructions for Side by Side Printing
- Print the notecards
- Fold each page in half along the solid vertical line
- Cut out the notecards by cutting along each horizontal dotted line
- Optional: Glue, tape or staple the ends of each notecard together
Antibody Antigen interactions
front 1 Explain what an antigen is | back 1 An antigen is any molecule that can be bound by an antibody. |
front 2 explain what an epitope is | back 2 An epitope (also called an “antigenic determinant”) is the region of the antigen that is bound (contacted) by an antibody. |
front 3 Describe the types of molecules that most biologically-relevant antigens comprised of? | back 3 no data |
front 4 antigens and epitopes | back 4 A single antigen may have many different or identical epitopes |
front 5 Describe the physical aspects of antibody/antigen binding. | back 5 no data |
front 6 Describe the chemical aspects of antibody/antigen binding | back 6 Hydrogen bonding ionic bonding hydrophobic interactions van der waals interactions |
front 7 Antibody X (IgG) binds to a bacterial protein called protein Q. Which of the following changes would likely result in the loss of antibody binding to protein Q? Chose all correct answers. a.) Changing the amino acid sequences of the CDRs of the two light chains. b.) Changing the conformation of the CDRs of the two heavy chains. c.) Changing the isotype of antibody X from IgG to IgA. d.) Replacing the two constant light chain domains (CL) with the constant light chain domain from a different antibody. e.) Changing the amino acids in protein Q that form the epitope bound by antibody X. | back 7 a.) Changing the amino acid sequences of the CDRs of the two light chains. b.) Changing the conformation of the CDRs of the two heavy chains. e.) Changing the amino acids in protein Q that form the epitope bound by antibody X. |
front 8 the difference between a linear epitope and a conformationally-dependent (discontinuous) epitope. | back 8 Linear: linear sequence of amino acids Discontinuous: The amino acids are being bond to the CDRs |
front 9 Explain the difference between antibody affinity and antibody avidity | back 9  Affinity: is the strength of binding between a single Fab region of an antibody and a single epitope Avidity: The collective strength of binding between multiple Fab regions of a single antibody (or antibody complex like pentameric Igm) with multiple epitopes |
front 10 Explain how the Coggin’s test is performed | back 10  |
front 11 Explain how the Coggin’s test is used to determine a horse’s prior exposure to equine infectious anemia virus (EIAV) | back 11 no data |
front 12 what is a conjugated antibody? | back 12 no data |
front 13 What types of molecules are commonly conjugated to antibodies? | back 13 no data |
front 14 Explain how an ELISA is performed | back 14 no data |
front 15 understand the roles of antibody and antigen in the assay | back 15 no data |
front 16 Explain how a Western blot is performed and the roles of antibody and antigen in the assay. | back 16 no data |
front 17 Explain what a primary antibody is and what a secondary antibody as
it pertains to the antibodies used in some types of | back 17 no data |