Chapter 4 Testbank

Chapter 4 Testbank - Chapter 4 The Three-Dimensional...

Info iconThis preview shows pages 1–3. Sign up to view the full content.

View Full Document Right Arrow Icon
Chapter 4 The Three-Dimensional Structure of Proteins Multiple Choice Questions 1. Overview of protein structure Pages: 114 - 115 Difficulty: 1 All of the following are considered “weak” interactions in proteins, except: A) hydrogen bonds. B) hydrophobic interactions. C) ionic bonds. D) peptide bonds. E) van der Waals forces. 2. Overview of protein structure Pages: 114 - 115 Difficulty: 2 The most important contribution to the stability of a protein’s conformation appears to be the: A) entropy increase from the decrease in ordered water molecules forming a solvent shell around it. B) maximum entropy increase from ionic interactions between the ionized amino acids in a protein. C) sum of free energies of formation of many weak interactions among the hundreds of amino acids in a protein. D) sum of free energies of formation of many weak interactions between its polar amino acids and surrounding water. E) stabilizing effect of hydrogen bonding between the carbonyl group of one peptide bond and the amino group of another. 3. Overview of protein structure Page: 115 Difficulty: 1 In an aqueous solution, protein conformation is determined by two major factors. One is the formation of the maximum number of hydrogen bonds. The other is the: A) formation of the maximum number of hydrophilic interactions. B) maximization of ionic interactions. C) minimization of entropy by the formation of a water solvent shell around the protein. D) placement of hydrophobic amino acid residues within the interior of the protein. E) placement of polar amino acid residues around the exterior of the protein. 4. Overview of protein structure Page: 115 Difficulty: 2 Pauling and Corey’s studies of the peptide bond showed that: A) at pH 7, many different peptide bond conformations are equally probable. B) peptide bonds are essentially planar, with no rotation about the C—N axis. C) peptide bonds in proteins are unusual, and unlike those in small model compounds. D) peptide bond structure is extraordinarily complex. E) primary structure of all proteins is similar, although the secondary and tertiary structure may differ greatly.
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Chapter 4 The Three-Dimensional Structure of Proteins 5. Overview of protein structure Page: 116 Difficulty: 3 In the diagram below, the plane drawn behind the peptide bond indicates the: A) absence of rotation around the C—N bond because of its partial double-bond character. B) plane of rotation around the C α —N bond. C) region of steric hindrance determined by the large C=O group. D) region of the peptide bond that contributes to a Ramachandran plot. E) theoretical space between –180 and +180 degrees that can be occupied by the φ and ψ angles in the peptide bond. 6.
Background image of page 2
Image of page 3
This is the end of the preview. Sign up to access the rest of the document.

Page1 / 9

Chapter 4 Testbank - Chapter 4 The Three-Dimensional...

This preview shows document pages 1 - 3. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online