-In a protein, the amino acid pairs below are near each other in the tertiary structure. For each pair briefly describe (10 words or less per pair) what kind of interaction is likely to occur at pH 7.4. If no interaction is likely, clearly state so. a. Cys-Arg b. Pro-Asp C. Ser-Phe d. His-Gln
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- What is the monomer of a nucleic acid macromolecule?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.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.
- 7/ Hemoglobin is an example of a protein with A. Primary structure only. B. two protein chains held together. C. a quaternary structure. D. primarily a B-pleated sheet structure.1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensation3. Why do we need to study the four levels of protein structure? Cite its practical use to our day-to-day life.
- 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.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.4. Which best describes the contribution of quaternary (4’) structure of polypeptides to the native conformation of proteins: a) Structure that results from intrachain interactions of amino B) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence acid side chains of amino acids from beginning to end of molecule
- 2- Some proteins contain additional amino acids that arise by modification of an amino acid already present in a peptide , examples include: a) Gamma Amino Butyric Acid. b) 5 - hydroxy Lysine c) 4 - hydroxy proline d) All of the above e) None of the above7. Native conformation of proteins may result from: a) hydrophobic interactions b) H-bonds c) ionic bonds d) covalent bonds e) all a-d may contribute to native conformation2 If a protein is predominantly made up of aliphatic and aromatic amino acids, which of the following is most likely true about such protein? Select the correct responses): a. It is a protein with a net negative charge b. It is most probably a structural protein. c. It is a protein that is cationic in nature. d. It is a protein that is hydrophobic in nature. e. It is most probably a catalytic protein. f. It is a water-solube protein. g. It is most probably a carrier protein.