4. Cis peptide bonds are rarely found in proteins because they are about 8 kJ/mole less stable than the trans isomer. However, in the rare instances where they are present, they are followed by a Pro residue. In fact, about 10% of the proline residues in proteins are found following a cis peptide bond. Why would a Pro following a cis peptide bond make a difference

4. Cis peptide bonds are rarely found in proteins because they are about 8 kJ/mole less stable than the trans isomer. However, in the rare instances where they are present, they are followed by a Pro residue. In fact, about 10% of the proline residues in proteins are found following a cis peptide bond. Why would a Pro following a cis peptide bond make a difference

Biology: The Unity and Diversity of Life (MindTap Course List)

14th Edition

ISBN:9781305073951

Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr

Chapter3: Molecules Of Life

Section: Chapter Questions

Problem 6SQ

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The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
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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 bond
1. 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.
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 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)Explain 3 benefits of proteins forming higher oligomeric states. 2) Why are peptide bonds planar?
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
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
3. How many amino acids are there in the polypeptide (protein)?
1.) What type of nucleic acid does this complex occur? 2.) How many 3',5'-Phosphodiester linkages were formed? from the complex of the given structure? Give ONLY the NUMBER of the linkages. 3.) Name the second complementary base from the 5' direction.
3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains 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 of amino acids from beginning to end of molecule