Certain 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
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Certain 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.
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- The Adaptive Immune Response Is a Specific Defense Against Infection Name the class of molecules that includes antibodies, and name the five groups that make up this class.What is the smallest unit of an antibody that can retain the specificity and binding affinity of the whole protein?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.
- Consider a pencil-shaped protein with two epitopes, Y (the “eraser” end) and Z (the “point” end). They are recognized by antibodies A1 and A2, respectively. Draw and label a picture showing the antibodies linking proteins into a complex that could trigger endocytosis by a macrophage.An antibody consists of four protein chains, two______chains and two_______ chains. Each is composed of a(n)_______ region and a(n)______region. The_______ regions form the binding site for antigens.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.
- 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 0Draw the general structure of an antibody and list the different classes as well as their abundanceAntibody 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.
- 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 following reactions are all antigen(Ag)-antibody(Ab) complexes. Match the description with the best reaction. Use each option only once.1. Antibodies react with soluble antigens and when they do, a complex forms that comes out of solution (e.g. is now insoluble).2. Reaction with insoluble antigens (a particle such as a cell with an antigen), rather than a soluble antigen.3. Antibodies coat antigens and enhances phagocytosis4. Antibodies with their antigen involve the complement proteins; can cause the invading organism to lyseAnswer choices to MATCH with the above sentences are:-Agglutination-Precipitin-Complement Fixation-OpsonizationDescribe the structure of an antibody.
