The five classes of immunoglobulin differ in …. Select one: a. None of the above b. Ability to bind various classes of antigens (viral, bacterial etc) c. Make up of the heavy and light chains d. Rate of mutation in the variable domain (i.e. speed at which each class can respond to a new antigen) e.
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The five classes of immunoglobulin differ in ….
None of the above
Ability to bind various classes of antigens (viral, bacterial etc)
Make up of the heavy and light chains
Rate of mutation in the variable domain (i.e. speed at which each class can respond to a new antigen)
Size of the variable domain
Step by step
Solved in 4 steps
- The Fab regions of an antibody are made of which protein chain? A) a heavy chain containing only constant regions B) a light chain containing variable and constant regions C) a heavy chain containing variable and constant regions D) both a light chain and a heavy chain containing variable and constant regions E) both a light chain containing variable and constant regions and a heavy chain containing only constant regionsDescribe the structure of immunoglobulin and the functions of the Fab and Fc portions.alpha:beta TCRs are membrane-bound proteins comprised of two polypeptides linked by a disulfide bond. Both polypeptide components of the alpha:beta TCR are members of the immunoglobulin superfamily, and each of their domains share structural similarity with regions of antibody proteins. However, due to the different functions of TCRs versus antibodies, the overall domain organization of the TCR is not the same as for an antibody. In the figure below, describe three features that are incorrect illustrations of the alpha:beta TCR.
- B cell-receptors differ from T cell-receptors in that ________. A) B cell-receptors are immunoglobulins similar to those that are secreted, whereas T cell-receptors are not immunoglobulins and are never secreted B) T cell-receptors are much smaller than B cell-receptors C) All of the choices reflect differences between B cell- and T cell-receptors. D) B cell-receptors are comprised of four polypeptides, whereas T cell-receptors are made up of two polypeptidesThe 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?What kind(s) of intermolecular interactions could be involved in the binding between an antibody and an antigen such as the spike protein?
- Which of the two antibodies shown in the figure below are most likely to have the same antigen-binding specificity? Explain your reasoningFor an Immunoprecipitation experiment:The cellular extract contains a protein labeled with a fluorescent dye, which emits green fluorescence under UV light. Explain your observations in IP-1, IP-2, and IP-3 tubes by considering the interaction among antibody 1 (or antibody 3), the fluorescent-labeled protein, and the protein-A agarose beads.What is the effect of the changes in the structure of the immunoglobulin G and its function of binding to and neutralizing/ tagging pathogens when there is an Increased production of metabolites in the blood that reduces its pH to < 6?
- It is often helpful to draw a complicated pathway in the form of a flow chart to visualize the multiple steps and the ways in which the steps are connected to each other. Draw the antibody-mediated immune response pathway that acts in response to an invading virus.T cells and B cells have many similarities in how they produce their highly diverse repertoire of antigen receptors, but one important difference between them is that B cell receptors can undergo somatic hypermutation to alter their affinity for antigen. This is known as ‘affinity maturation’, and the result is that the pool of B cells specific for a particular microbe will increase their binding affinity. T cells do not engage in either somatic hypermutation or affinity maturation. Why not? What potential harm could come from allowing T cells to alter the affinity of their TCRs after they have already left the thymus and have become activated in a lymph node or spleen?In terms of a virus, how could injecting an mRNA sequence trigger an immune response. be sure to also explain how antibodies, antigens, t cells, b cells, and immune memory work within this situation.