6. How are amino acids linked together in a protein molecule? Write the general structure of the tripeptide lys-phe-meth. Show their peptide bonds. Illustration: Label the amino acids.
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Q: 6) What is the cognate a-keto acid of alanine? You may have to look at alanine.
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- What is the monomer of a nucleic acid macromolecule?6.All of the following types of interactions cooperate in stabilizing the tertiary structures of globular proteins except____. a.Disulphide bond b.Hydrogen bond c.Ionic interactions d.Peptide bond1. Which of the following forms of lysine would you expect to predominate at low pH, neutral pH and high pH? 2. One of the 20 amino acids is unusual in that its side chain contains a ring that incorporates the amine functional group of the amino acid. What is the name of this amino acid? Write the chemical structure of this amino acid at physiological pH.
- 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. Explain how each primary structure of a protein affects its properties and how denaturation changes the structure. 2. Explain how each secondary structure of a protein affects its properties and how denaturation changes the structure.
- 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 above1.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.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.What reactive groups are involved in the formation of a peptide bond?2.A molecule of what substance must be removed in order to form a peptide bond?1. What kind of bond links a base to some sugar? Is the sugar an alpha or beta anomer? In what position(s) of the sugar does this occur? In what position(s) of the base does this occur?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) Condensation
