Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 7, Problem 2P
Certain antibodies have been shown to bind only to the folded structure of their target protein ligand; yet others will bind to both the folded and denatured states of the same protein ligand. Explain this observation.
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Certain antibodies have been shown to bind only to the folded structure oftheir target protein ligand; yet others will bind to both the folded and denatured states of the same protein ligand. Explain this observation.
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.
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.
Chapter 7 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 7 - Prob. 1PCh. 7 - Certain antibodies have been shown to bind only to...Ch. 7 - Antibodies raised against a macromolecular antigen...Ch. 7 - Prob. 4PCh. 7 - Prob. 5PCh. 7 - Prob. 6PCh. 7 - Prob. 7PCh. 7 - Prob. 8PCh. 7 - Prob. 9PCh. 7 - Prob. 10P
Ch. 7 - Prob. 11PCh. 7 - Prob. 12PCh. 7 - Prob. 13PCh. 7 - Suppose your biking partner claims that...Ch. 7 - Prob. 15PCh. 7 - An antibody has been isolated that binds to...Ch. 7 - A typical relaxed sarcomere is about 2.3 m in...Ch. 7 - Each gram of mammalian skeletal muscle consumes...Ch. 7 - A few hours after the death of an animal, the...
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- 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.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_forwardEach immunoglobulin (Ig) domain is composed of a structure known as a ‘b-sandwich,’ which consists of two b sheets covalently linked by a disulfide bond. Only a subset of the ~110 amino acids in each domain are required to establish this overall structure, and it is these amino acids that are highly conserved when comparing Ig domains to each other. What might be the advantage of this structure for use as antibody variable domains?arrow_forward
- The F ab fragment of an antibody molecule has essentially the same affinity for a monovalent hapten as does intact IgG. (a) What is the smallest unit of an antibody that can retain the specificity and binding affinity of the whole protein? (b) Design a compact single-chain protein that is likely to specifically bind antigen with high affinity.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_forwardExperiments are performed to analyze protein tyrosine phosphorylation in response to TCR stimulation. For these experiments, T cells are stimulated with anti-CD3 antibody, and then lysates are prepared and run on a protein (SDS-PAGE) gel to separate the proteins by molecular weight. The proteins are transferred from the gel to a membrane for immunoblotting using an antibody that binds to all phosphorylated tyrosine residues in any protein; this antibody is called ‘anti-phospho-tyrosine antibody,’ and is abbreviated as anti-P-Y. The results are shown in the figure below. You confirm that the mutant T cells express normal levels of all the proteins detected in the WT cells, including PLC-g, SLP-76, ITK, ZAP-70, LCK, LAT, and the CD3 and TCRz proteins. Based on these data, which of the following proteins (biotin, hygromycin, and streptavidin) can rule out its presence? Briefly explain your answer. What protein is most likely defective in the mutant cells and why? For the protein you…arrow_forward
- 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-Opsonizationarrow_forwardWhy would attaching an enediyne- containing molecule to an antibody be an attractive way to treat cancer cells?arrow_forwardAntibody 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.arrow_forward
- 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 oligosaccharidesarrow_forwardOur immune system makes many different proteins that protect us from viral and bacterial infection. Biotechnology companies must produce large quantities of these immune proteins for human testing and eventual sale to the public. To this end, their scientists engineer bacterial or human cell cultures to express these immune proteins. Explain why proteins isolated from bacterial cultures are often inactive, whereas the same proteins isolated from human cell cultures are active (functional).arrow_forwardT 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. 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?arrow_forward
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