Concept explainers
What properties of proteins make them suitable molecules from which to make antibodies?
Immunoglobulins (Igs), also termed as antibodies, are glycoprotein molecules made by plasma cells (white blood cells). Igs play an important role in the immune response by particularly identifying and binding to antigens, like bacteria and viruses and thereby aids in destructing them. Igs are classified into five types, namely IgA, IgD, IgE, IgG, and IgM.
Explanation of Solution
Immunoglobulins are proteins that need to be able to form binding surfaces, called idiotopes. These binding surfaces show great chemical diversity, to be complementary with a great diversity of antigen binding sites, called epitopes, on antigens. In general, proteins have 20 amino acids and also possess great structural diversity, which is needed to make antibodies. Nucleic acids and lipids are by comparison more repetitive.
Want to see more full solutions like this?
Chapter 34 Solutions
Prescott's Microbiology
- What kind(s) of intermolecular interactions could be involved in the binding between an antibody and an antigen such as the spike protein?arrow_forwardWhat is the basic structure of the antibody molecule?arrow_forwardWhy would attaching an enediyne- containing molecule to an antibody be an attractive way to treat cancer cells?arrow_forward
- What is the smallest unit of an antibody that can retain the specificity and binding affinity of the whole protein?arrow_forwardCertain antibodies bind solely to the folded structure of their target protein ligand, whereas others bind to both the folded and denatured forms of the same protein ligand. Explain what you've noticed.arrow_forwardWhat are chimeric antigen receptors (CARs) ?arrow_forward
- 1) What is an obvious physical difference between an immunoglobulin (an antibody) and glucose (a monosaccharide)? 2) Draw a sketch of a method that could be used to separate immunoglobulins from glucose utilizing the physical differences between the molecules that you mentioned in question 1.arrow_forwardWhat type of molecule forms the antibodies found in the human immune system?arrow_forwardAntibodies are effective against bacteria as well as viruses, but some bacteria produce an enzyme that cuts immunoglobulin G molecules right at the “bend” to separate each antigen-binding “arm” from the “stem.” (a) What type of bond is broken by the bacterial enzyme and what type of reaction does this enzyme catalyze? (b) Would the action of the bacterial enzyme affect the ability of immunoglobulins to cross-link bacterial cells?.arrow_forward
- You are an energetic immunology student who has isolated protein X, which you believe is a new isotype of human immunoglobulin. What structural features would protein X have to have to be classified as an immunoglobulin? Make diagram to illustrate your answer.arrow_forwardWhat is the function of carbohydrate groups present in collagen? Where are the carbohydrate units located in collagen? What is the role of vitamin C in the biosynthesis of collagen? What is the difference between an antigen and an antibody? What is immunoglobulin? Describe the structural features of a typical immune-globulin molecule? Describe the process by which blood immunoglobulins help protect the body from invading bacteria and viruses. Describe the general overall structure of plasma lipoprotein. In what chemical form does cholesterol usually exist in the bloodstream?arrow_forwardThe ends of each heavy chain and light chain in an immunoglobulin make up the antigen-binding sites. The end of one of these chains is shown here. Biochemists tend to classify protein structures into four groups: mostly alpha, mostly beta, mixed alpha and beta, or neither alpha nor beta. Based on the model shown here, how would you classify this part of the immunoglobulin protein? The loopy polypeptide segments at the very top of the structure shown are the segments that actually contact the antigen. Would you expect these binding segments to be rigid or flexible?arrow_forward