Which of the following are elements of the structure of antibodies? Select all that apply. The antigen-binding sites are unique to each antibody. Each antibody has three binding sites for antigens. The antigen-binding sites of each antibody can bind to multiple antigen types. Four polypeptide chains are joined in a Y-shaped configuration.
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- Before the mechanism for generating antibody diversity had been established, a mechanism based on protein folding around an antigen was proposed, primarily by Linus Pauling. In this model, antibodies that had different specificities had the same amino acid sequence but were folded in different ways. Propose a test of this model.Antibody binding to a pathogen surface is greatly enhanced when both antigen-binding sites of the antibody are engaged at once, a feature known as bivalent binding. It is possible for antibodies to bind bivalently to a wide variety of components on many different pathogen surfaces due to the flexibility in the protein at the hinge region and at the V–C junction.Draw a schematic diagram of a typical IgG molecule and label each of the following parts: H chains, L chains, intrachain disulfide bonds, hinge, Fab, Fc, and all the domains. Indicate which domains are involved in antigen binding.
- Some pathogenic microorganisms encode proteins, such as the Staphylococcus Protein A, that bind to immunoglobulin constant region domains with high affinity. These microbial proteins provide a benefit to the microorganism by: Preventing antibodies bound to the microbe from binding to Fc receptors on phagocytes Blocking the binding of anti-microbial antibodies to the pathogen surface Cleaving the antibody into fragments that separate the antigen-binding region from the effector function Inducing aggregation of the anti-microbial antibodies by multivalent binding to the pathogen-derived protein Preventing the antibody from neutralizing the pathogenWhich of the following are elements of the structure of antibodies? Select all that apply. The antigen-binding sites of each antibody can bind to multiple antigen types. Four polypeptide chains are joined in a Y-shaped configuration. Each antibody has three binding sites for antigens. The antigen-binding sites are unique to each antibody.Neutralizing antibodies are effective at preventing infection or toxicity mediated by pathogens or their toxic products. In fact, nearly all vaccines currently in use function by eliciting neutralizing antibodies. One example is the tetanus vaccine, in which neutralizing antibodies are generated against an inactivated form of the tetanus toxin (the tetanus toxoid). The most important feature of a neutralizing antibody is having high affinity for the antigen. being efficient at activating the complement cascade. having a high degree of multivalency, such as being a pentamer or hexamer of immunoglobulin monomers. being present at a high concentration in the circulation. 0 0 0 0
- Observe the structure of antibodies below that has four protein subunits. Explain why we only see two (not four) bands on the SDS PAGE gel.How are antibodies unique? Please discuss the structure of an antibody. What are the V and C regions? Discuss how the few hundred genes involved are capable of making endless amounts of antibodies. Besides medical treatment what is another way antibodies can be used?The antibody surface involved in antigen binding varies depending on the size and nature of the antigen. This surface can be concave or flat, and sometimes, can have extended protrusions. This is accomplished by: Flexibility in the hinge regions of the antibody allowing rotation of the antigen-binding sites Some antibodies using V region framework sequences instead of the CDRs to bind antigen The ability of different CDR sequences to form many structurally distinct shapes and surfaces The ability of the same heavy chain to pair with different light chains The differential usage of κ versus λ light chains, as κ chains form concave
- What is the variable region of an antibody? The hypervariable or complementarity-determining region? The constant region?For the diagram below, all of the following statements are true EXCEPT: Antigen- binding site V C Heavy chain V Light chain S.S. Fc (stem) region c C Hinge region None of the other four answers (All are true statements) Antibodies (Immunoglobulins) are composed of four protein molecules, two identical "light" chains and two identical "heavy" chains Antigens bind to the "stem", composed of the constant regions of the two "heavy" chains The variable (V) regions form the antigen binding sites The constant (C) regions determine class of antibodyDiagram the structure of an antibody. What parts bind toantigens? Why does each antibody bind only to one or afew specific antigens?