Please help me with this question. How many amino acid residues are in the heavy and light chains of the Fab fragment, and how many amino acid residues are in lysozyme?
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Proteins
We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains thousands and thousands of proteins, each with specific functions. Some help in the formation of cellular membrane or walls, some help the cell to move, others act as messages or signals and flow seamlessly from one cell to another, carrying information.
Protein Expression
The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry, and protein research laboratories.
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- If an extra nucleotide is inserted in the first exon of the beta globin gene, what effect will it have on the amino acid sequence of the globin polypeptides? Will the globin most likely be fully functional, partly functional, or nonfunctional? Why?Using sickle-cell anemia as an example, describe what is meant by a molecular or genetic disease. What are the similarities and dissimilarities between this type of a disorder and a disease caused by an invading microorganism?Find a method that uses some form of HPLC for the analysis of proteins. What was the stationary phase used? How does this kind of stationary phase separate the proteins? What kind of mobile phase was used? Was the method isocratic or was a gradient used? How were the proteins detected?
- What are the primary proteolytic enzymes used to degrade immunoglobulin molecules into definable fragments to facilitate the study of their structure? Beside each peptide bond-splitting enzyme, indicate the number of fragments they produce after digestion.Jack is applyng to Gate's foundation for a grant to make a high affinity, humanized monoclonal antibody that could neutralize venom, a 7 kDa protein of 62 amino aicds, from cobra snakes. He argues that many people in tropical areas are bitten by the poisonous snakes and may need injection of this life-saving anitbody more than once. His friend has successfully purified the 7kDA venom protein expressed in E. coli in a large quantity and will give him whatever he needs for his project. Assume that he recovers four anti-venom monoclonal antibodies. What is the method he can use to identify the one with the highest affinity to the venom?Jack is applyng to Gate's foundation for a grant to make a high affinity, humanized monoclonal antibody that could neutralize venom, a 7 kDa protein of 62 amino aicds, from cobra snakes. He argues that many people in tropical areas are bitten by the poisonous snakes and may need injection of this life-saving anitbody more than once. His friend has successfully purified the 7kDA venom protein expressed in E. coli in a large quantity and will give him whatever he needs for his project. Among more than 100 candidates, what can he do to identify those that recognize the venom?
- Explain why release factors are called “molecular mimics.”In eukaryotic cells secreted proteins are targeted first to the endoplasmic reticulum and then pass through the Golgi, before being released from secretory vesicles into the extracellular space. A much simpler route would be for ribosomes synthesising secretory proteins to be targeted to a translocon in the plasma membrane, with the protein being secreted directly as it is translated. List three potential advantages of the former, more circuitous, route for protein secretion over the simpler, more direct, alternative route suggested.Amino acid sequence analysis of all of the peptides found in a single IgG antibody would reveal unique peptide sequences totaling ~600–700 amino acids. Using this estimate, the predicted molecular weight of an antibody protein would be ~70–75 kDa. Yet, an intact antibody protein has a molecular weight of ~150 kDa. The explanation for this discrepancy is: IgG antibodies have many more heavy amino acids in them than most other proteins. Each IgG antibody is a complex of two identical light chains and two identical heavy chains. IgG antibodies tend to aggregate together during purification, thereby distorting molecular weight estimates. Each IgG antibody is a complex of four identical polypeptides. IgG antibodies are produced as dimers of two identical IgG monomers.
- Describes a method known as Western blotting that can be used to detect a polypeptide that is translated from a particular mRNA. In this method, a particular polypeptide or protein is detected by an antibody that specifically recognizes a segment of its amino acid sequence. After the antibody binds to the polypeptide within a gel, a secondary antibody (which is labeled) is used to visualize the polypeptide as a dark band.For example, an antibody that recognizes α-galactosidase A couldbe used to specifically detect the amount of α-galactosidase A proteinon a gel. The enzyme α-galactosidase A is defective in individuals with Fabry disease, which shows an X-linked recessive pattern of inheritance. Amy, Nan, and Pete are siblings, and Pete has Fabry disease. Aileen, Jason, and Jerry are brothers and sister, and Jerry has Fabry disease. Amy, Nan, and Pete are not related to Aileen, Jason, and Jerry. Amy, Nan, and Aileen are concerned that they could be carriers of a defective…Consider the genes that specify the structure of hemoglobin. Arrange the following events in the most likely sequence in which they would take place.a. Anemia is observed.b. The shape of the oxygen-binding site is altered.c. An incorrect codon is transcribed into hemoglobinmRNA.d. The ovum (female gamete) receives a high radiationdose.e. An incorrect codon is generated in the DNA of ahemoglobin gene.f. A mother (an X-ray technician) accidentally stepsin front of an operating X-ray generator.g. A child dies.h. The oxygen-transport capacity of the body is severelyimpaired.i. The tRNA anticodon that lines up is one of a typethat brings an unsuitable amino acid.j. Nucleotide-pair substitution occurs in the DNA of agene for hemoglobinThree different ligands, Ligand Q, Ligand T, and Ligand W, bind to the same protein but with different affinity: The association constant (Ka) for the binding of Ligand Q to the protein is 0.033 nM-1. The fractional saturation (Y) of the protein is 0.20 when the concentration of Ligand T is 1.25 nM. The fractional saturation (Y) of the protein is 0.80 when the concentration of Ligand W is 72 nM. Given this information, Calculate Kd for the binding of each ligand to this protein. Which ligand binds with greatest affinity? Which ligand binds with the lowest affinity?