You have been asked to engineer a protein (which is not an immunoglobulin) that is capable of binding to a given protein target. Devise a strategy and discuss the main molecular screening approaches required.
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1) You have been asked to engineer a protein (which is not an
immunoglobulin) that is capable of binding to a given protein target.
Devise a strategy and discuss the main molecular screening
approaches required.
Step by step
Solved in 2 steps
- Hybridoma technology allows one to generatemonoclonal antibodies to virtually any protein. Why isit, then, that genetically tagging proteins with epitopes issuch a commonly used technique, especially since an epi-tope tag has the potential to interfere with the function ofthe protein?If I purchase a mouse anti GAPDH antibody what will it bind to?Explain how site-specific recombination of the κ light-chain gene increases antibody diversity.
- Describe three examples of how antibodies are used as reagents in cell biology and molecular biology.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.One strategy for vaccine development currently under investigation is the use of pathogen-derived T cell epitopes as a component of the vaccine. For viral pathogens, implementing this strategy involves scanning the predicted amino acid sequences of the viral proteins for likely peptide epitopes that would bind to MHC class I and MHC class II molecules. In addition to the complication of MHC sequence polymorphism in the human population, another complication of this strategy for peptide epitopes that would bind to MHC class II proteins is: The importance of viral proteins containing peptides that are cleaved into 8–10 amino acid long fragments. The ability of viruses to mutate their proteins to avoid MHC anchor residue sequences. The fact that long peptides (>13 amino acids) are rapidly degraded in cells. The fact that MHC class II proteins are intrinsically stable, even in the absence of binding to a peptide. The absence of defined sequence motifs that predict peptide binding to…
- If the heavy chain of an antibody is approximately 450 amino acids long, how much DNA would be required to encode 10° separate heavy chain genes?Regarding the production of recombinant monoclonal antibodies, it is CORRECT to state that: * (JUST ONE STATEMENT IS CORRECT) (A) Chimeric and humanized antibodies differ in relation to the percentage of sequence of the constant chain of molecules from the human genome (B) Chimeric antibodies are industrially produced by joining purified protein fragments of the Fab fraction of murine antibodies and the constant portion of human antibodies. (C) When using cells dependent on the DHF amplification system, we must use a vector containing the coding information of the light and heavy chains and another vector that contains the coding sequence of the enzyme dihydrofolate reductase (D)The industrial purification of monoclonal antibodies should preferably use an initial step based on the use of affinity columns, which will bind the antibodies by the Fc fraction (E) The use of amplification systems such as GS and DHFR has as main objective to make the production of monoclonal antibodies…Humanized monoclonal antibodies are best described as a. antibodies made in mice in which the mouse antibody genes have been replaced with human equivalents b. human antibodies in which the CDR loops have been replaced by mouse-derived CDRs of the desired specificity c. antibodies made in culture by human hybridomas d. antibodies containing mouse Fab regions of both the heavy and light chain and human Fc regions e. antibodies containing human Fab regions of both the heavy and light chain and mouse Fc regions.
- How does the formation of a colored product in the wells durin a ELISA ASSAY demonstrate characteristics of antigen-antibody recognition? How might concentration of antigen and/or antibody affect the formation of the blue color formation expected.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…why would there be some additional bands on an immunoblot that do not match the molecular weight of the targeted protein (LDH)? what could be the problem if LDH positive bands showed up that were smaller than the normal size of LDH? how about if they were 2X larger?