True/False: The antibody protein has two functional domains, one for antigen binding and a second to confer specific effector functions. These two functional domains are encoded by the antibody light chain and antibody heavy chain polypeptides, respectively

True/False: The antibody protein has two functional domains, one for antigen binding and a second to confer specific effector functions. These two functional domains are encoded by the antibody light chain and antibody heavy chain polypeptides, respectively

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 11QP: It is often helpful to draw a complicated pathway in the form of a flow chart to visualize the...

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True/False: The different classes of immunoglobulins differ in the sequences of their heavy chain constant regions. As a result, each class of antibody has distinct effector functions. Nonetheless, they are all found at about equal concentrations in the serum of healthy individuals.
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
What is the smallest unit of an antibody that can retain the specificity and binding affinity of the whole protein?
Antibody heavy and light chain polypeptides consist of repeated domains, each of which is ~110 amino acids and folds up into a compact three-dimensional structure known as an ‘immunoglobulin domain.’ These immunoglobulin domains are: Mixed and matched between different antibody heavy and light chains to produce variability Always identical to each other within a single antibody heavy chain or light chain polypeptide Always differ in amino acid sequence between different light chain polypeptides in both of the two light chain immunoglobulin domains Similar but not identical in amino acid sequence when comparing the domains in a single heavy chain polypeptide Identical in amino acid sequence for every domain when comparing different antibody heavy chain polypeptides to each other
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?
True or false: the antigen binding site of an antibody is found in the variabe region of the antibody.
Antibody diversity is generated by multiple mechanisms, each of which contributes to the generation of antibodies with up to 1011 different amino acid sequences in their antigen-binding sites. Several of these mechanisms involve changes in the DNA sequences encoding the antibody heavy and light chain proteins. One mechanism that does not rely on changes to the DNA within the immunoglobulin heavy and light chain gene loci is, instead, dependent on: The contributions of amino acids from both the heavy chain and the light chain to form the antigen-binding site The random usage of V, D, and J gene segments to form the heavy chain V region sequence The random usage of k light chains versus l light chains to pair with the heavy chain The activity of TdT to add random nucleotides at the junctions between the V, J, and D region sequences The fact that heavy chain V regions contain an extra gene segment encoded by the D region compared to light chain V regions
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-Opsonization
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.
Experiments 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…
You can choose one or more than one option Antibodies: IMMUNOLOGY basic have two identical antigen-binding sites. consist of two identical heavy chains and two identical light chains. are secreted by plasma cells are produced by T lymphocytes during adaptive immune response can bind their constant heavy chain region to phagocytes Which of the following proteins are transmembrane proteins? CELL BIOLOGY basic integrin oestrogen receptor phospholipase C adenosine triphosphate (ATP) synthase growth factor receptor What are the correct statements? MOLECULAR BIOLOGY advanced A mutation located within a promoter can change the gene expression. An mRNA can be differentially spliced according to the tissue. RNA transcribed by the RNA polymerase II are translated The end of the transcription process requires a specific DNA sequence A reverse transcriptase can polymerise either a DNA or an RNA strand. Which of the following cells kill other cells by exocytosis of…
True/False: MHC class I surface expression is dependent on an abundant source of pathogen-derived peptides. Thus, in uninfected cells, nearly all of the MHC class I proteins are degraded and never reach the cell surface.