In an antibody, the heavy chain polypeptides are attached to the light chain polypeptides through disulfide bonds to form the structure of the protein.
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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.Why antibodies raised against a native protein sometimes fails to bind to the corresponding denatured protein?Explain your answeOn an antibody the variable regions form the __________________.
- Given the following protein mixture, answer the following questiona. using hydrophobic interaction chromatography, what is the protein that will be eluted first|b. using affinity chromatography the protein that will be eluted LAST in an antigen containing column isc. the protein with the least migration in SDS-PAGE is?What is the smallest unit of an antibody that can retain the specificity and binding affinity of the whole protein?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.
- 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?Labs that do a lot of Western blots often have hundreds of primary bodies but only two or three secondary antibodies. Why? I understand that secondary antibody aids in the detection, sorting or purification of target antigens by binding to the primary antibody which directly binds to the target antigen. However, I don't undrstand why there are only two or three secondary antibodies available in the laboratory. Glad if the expert would advise.An injection contains 5 million international units (MIU) of interferon alpha-n3 (ALFERON N) proteins per milliliter. The recommended dose is 0.05 mL. The literature states that the activity of interferon alpha-n3 is approximately equal to 2.6 × 108international units/mg of protein. Calculate (a) the number of international units and (b) the micrograms of interferon alfa-n3 proteins administered per dose.
- 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 oligosaccharidesAntibody X binds to a polypeptide antigen with the following sequence: Leu-Ala-Phe-Val-Leu-Trp-Ala Based upon the sequence of the antigen, what amino acid in Antibody X would you expect to bind the antigen. ARG ILE ASP SER O LYS Provide a reason for why you chose the above amino acid based upon the biochemical properties of the antigen and the amino acid you chose.True or False: An IgM monomer can bind as many as 10 epitopes?