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- 1. What is hemoglobinopathy? What is sickle-cell anemia? Explain the concept relating to protein structure. 2. How does the oxygen-carrying functions of myoglobin differ from that of hemoglobin?1.Here is an oligomeric protein, which has two binding sites:1)Write the formulas of side chains of amino acids which are located in binding sites and suggest two ligands,which can be bound with this protein. 2) Name the types of bonds which will be formed between the ligands and amino acids of binding sites.3)Give the definition of quaternary structure. What do you know about the properties of proteins with the quaternary structure?1. In a protein, why does when Ala is replaced with Ile, it loses its activity but when Lys is replaced by Arg and Leu to Ile, it only has little effect on protein structure and function? Explain. 2. Why do proteins cannot be denatured reversibly when they are chemically altered to change the chemical composition of certain side chains? Explain.
- 1. Sickle cell anemia results from a substitution of a valine for a glutamic acid. What do you expect the effect might be if the mutation were to have placed a leucine at that site? An aspartic acid? 2. Of the following amino acids, glycine, isoleucine, and lysine, which would you expect to be the most soluble in an acidic aqueous solution? Which the least? 3. How many structural isomers could be formed from a molecule with the formula C5H12? C4H8?1) What are the four levels of protein folding. How do you distinguish those different levels? What can denature a protein? 2) What are detergents and why are they useful? How do they basically work? 3) What is meant by amphipathic? What is an example of this?1. Consider the following α helix from myoglobin at pH 7. Gln-Gly-Ala-Met-Asn-Lys-Ala-Leu-Glu-His-Phe-Arg-Lys-Asp-Ile-Ala-Ala-Lys-Tyr(a) Label amino acids in the polypeptide above as follows: p for polar and uncharged, np for non polar, – for negatively charged, and + for positively charged.(b) How many complete turns are there in this helix?(b) Which side chains are likely to be on the side of the helix that faces the aqueous solvent? Why?(c) Which side chains are likely to face the interior of the protein? Why?
- 1. Theoretically, a protein could assume a virtually infinite number of configurations and conformations. Suggestseveral features of proteins that drastically limit the actual number. 2. What are the greatest structural features that differentiate sphingolipids from phosphoglycerides? 3. High levels of glucose-6-phosphate inhibit glycolysis. If the concentration of glucose-6-phosphate decreases,activity is restored. Why?6. Which amino acid would most likely be found on the surface of a protein molecule at physiological pH? a. Isoleucine b. Lysine c. Alanine d. Proline 7. Which of the following statements about terpenes is NOT true? a. They are a type of terpenoid. b. They all contain double bonds. c. They are all made up of 5-carbon units. d. They all contain oxygen. 8. How are the plasma membranes of mammalian and bacterial cells similar? a. They typically contain cholesterol. b. They have negatively charged lipids on their surfaces. c. They contain lipids that are involved in signal transduction. d. They are made up of many different types of phospholipids.3. How many amino acids are there in the polypeptide (protein)?
- 1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic point of the amino acids are as follows: histidine:7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.1.a.If this molecule was the side chain of an amino acid, in a protein, what tertiary structure stabilizers could be present? b.Make a key and use color to highlight what part of you structure can be stabilized in each manner?1.Which levels of protein structure organization are lost during hydrolysis and denaturation? 2.What is the Beer-Lambert's Law? Why is it relevant to the quantitative analysis of proteins? 3.What are the other protein components of milk aside from casein?