3. Draw the chemical structure of cholesterol and state its functions4. Explain in detail the structural organization of proteins5. The human hemoglobin is a tetrameric protein of about 64.5 KDa, consisting of two a-chains and two B-chains tightly bound.a) Calculate the number of amino acids present in the a-chainsb) What is the length of each B-chain?c) What is the sum of the length of the two a-chains?d) Find the length of the tetrameric protein hemoglobin assuming its all an alphahelical structure.6. Study the polypeptide structure sequence of a B-strand shown belowLys-Gly-Asp-Trp-Ser-Glua) Draw the chemical structure of the polypeptide. Indicate on the structure thebackbone and peptide bondsb) Calculate the weight of the protein in KDac) Calculate the length of the protein.

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Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter3: Biological Molecules: The Carbon Compounds Of Life

Section: Chapter Questions

Problem 13TYK

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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. Discuss how the pH and temperature affect the solubility of protein. 2. Explain "salting-in" in your own words.
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?
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.
1. a. Explain why the melting point of palmitic acid (16 carbons, no double bonds) is slightly lower thanthat of stearic acid (18 carbons, no double bonds). Explain why the melting point of oleic acid (18carbons, one double bond) is lower than that of stearic acid b. A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, phosphatidylserine, andphosphatidylethanolamine was applied to a hydrophobic interaction chromatography column. Thecolumn was washed with a high salt buffer, and the lipids were then eluted with decreasing saltconcentrations. In what order would the lipids be eluted from the column? Explain your answer.
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.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.
3. A biochemist purified a protein from the bloodstream and determined its molecular weight under several conditions. In 8 M urea, which denatures the polypeptide chain, the molecular weight of the protein was 150,000 Da. She found that under reducing conditions the molecular weight of the protein was 75,000 Da, while under oxidizing conditions the molecular weight of the protein was 150,000 Da. Explain these results.
1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric 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. Draw the structure of a cholesterol ester where cholesterol is esterified with palmitic acid. is this polar or nonpolar acid 2. Draw the strucutre of lecithin containing stearic acid on carbon 1 and arachidonic acid on carbon 2 of glycerol. is this polar or nonpolar acid 3.Disccuss the medical sginificance of cholesterol , cholesterol ester,l ecithin and choline . 4. Give examples of phosphoglycerides and sphingolipids of biological importance .

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