Antibodies are composed of two types of peptides, heavy chains and light chains. One of the major classes of antibody molecules is immunoglobulin G (IgG). Two heavy chains and two light chains form one IgG molecule. Classify each statement as describing the heavy chains, light chains, or both chains of IgG. Heavy chains are found in the Fe fragment contain multiple constant domains Light chains contain only one constant domain contain multiple variable domains Both chains are found in the Fab fragment contain only one variable domain form the antigen-binding site

Antibodies are composed of two types of peptides, heavy chains and light chains. One of the major classes of antibody molecules is immunoglobulin G (IgG). Two heavy chains and two light chains form one IgG molecule. Classify each statement as describing the heavy chains, light chains, or both chains of IgG. Heavy chains are found in the Fe fragment contain multiple constant domains Light chains contain only one constant domain contain multiple variable domains Both chains are found in the Fab fragment contain only one variable domain form the antigen-binding site

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter17: Genes And The Immune System

Section: Chapter Questions

Problem 12QP: The Adaptive Immune Response Is a Specific Defense Against Infection Describe the genetic basis of...

See similar textbooks

Similar questions

Why antibodies raised against a native protein sometimes fails to bind to the corresponding denatured protein?Explain your answe
For 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.
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.
The 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 is the smallest unit of an antibody that can retain the specificity and binding affinity of the whole protein?
Treatment of antibodies with a particular protease clips theheavy chains in half, releasing the two arms of the Y-shapedmolecule. How might the antibodies continue to function?
When a mixture of different IgG antibody proteins are treated with the enzyme papain, each antibody is cleaved into three roughly equal size fragments. From each original antibody, two of the three fragments are identical to each other, and represent the ‘arms’ of the antibody ‘Y’. These fragments are known as Fab fragments. The third fragment is known as the Fc region, because this fragment will crystallize when purified. The reason a mixture of Fc fragments will crystallize is because: It is the only part of the antibody protein that can easily be purified at the high concentrations needed for crystallization. It has no disulfide bonds holding the domains together, as disulfide bonds will inhibit crystallization. It is the only fragment of the antibody that still has disulfide bonds, so it remains intact during the crystallization process. The Fc fragments of IgG are much more water soluble than the Fab fragments. All Fc fragments generated from a mixture of IgG molecules have the…
For many years it was a complete mystery howcytotoxic T cells could see a viral protein that seemed to bepresent only in the nucleus of the virus-infected cell. Theanswer was revealed in a classic paper that took advan-tage of a clone of T cells whose T cell receptor was directedagainst an antigen assoicated with the nuclear protein ofthe 1968 strain of influenza virus. The authors of the paperfound that when they incubated high concentrations ofcertain peptides derived from the viral nuclear protein, thecells became sensitive to lysis by subsequent incubationwith the cytotoxic T cells. Using various peptides from the1968 strain and the 1934 strain (with which the cytotoxic Tcells did not react), the authors defined the particular pep-tide responsible for the T cell response (Figure Q24–1).A. Which part of the viral protein gives rise to thepeptide that is recognized by the clone of cytotoxic T cells? Why do not all viral peptides sensitize the target cells forlysis by the cytotoxic T…
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 regions
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.
Like many proteins that do their jobs outside of cells, immunoglobulin G is a glycoprotein. The oligosaccharide chains are attached to the “stem” of the Y-shaped molecule and are believed to help protect the protein. Based on your understanding of carbohydrates, explain why it would not make sense for the immunoglobulin’s two antigen-binding arms to have attached oligosaccharides
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.