bonds within a peptide backbone with free rotation

#Bonds within a peptide backbone with free rotation free

Protein secondary structure Page: 117 Difficulty: 2 Ans: C Roughly how many amino acids are there in one turn of an A) B) C) D) E) 1 2 3 4 10 Chapter 4 The Structure of Proteins 41 14.

#Bonds within a peptide backbone with free rotation free

Overview of protein structure Page: 116 Difficulty: 2 Ans: A Which of the following pairs of bonds within a peptide backbone show free rotation around both bonds? A) B) C) D) E) and and and and and 8. Overview of protein structure Page: 116 Difficulty: 2 Ans: D Which of the following best represents the backbone arrangement of two peptide bonds? A) B) C) D) E) 7. theoretical space between and degrees that can be occupied the and angles in the peptide bond. region of the peptide bond that contributes to a Ramachandran plot. region of steric hindrance determined the large group. Overview of protein structure Page: 116 Difficulty: 3 Ans: A In the diagram below, the plane drawn behind the peptide bond indicates the: A) B) C) D) E) absence of rotation around the bond because of its partial character. Chapter 4 The Structure of Proteins 39 5. primary structure of all proteins is similar, although the secondary and tertiary structure may differ greatly. peptide bond structure is extraordinarily complex. peptide bonds in proteins are unusual, and unlike those in small model compounds. peptide bonds are essentially planar, with no rotation about the axis. Overview of protein structure Page: 115 Difficulty: 2 Ans: B Pauling and studies of the peptide bond showed that: A) B) C) D) E) at pH 7, many different peptide bond conformations are equally probable. placement of polar amino acid residues around the exterior of the protein. placement of hydrophobic amino acid residues within the interior of the protein. minimization of entropy the formation of a water solvent shell around the protein. The other is the: A) B) C) D) E) formation of the maximum number of hydrophilic interactions.

One is the formation of the maximum number of hydrogen bonds. Overview of protein structure Page: 115 Difficulty: 1 Ans: D In an aqueous solution, protein conformation is determined two major factors. E) stabilizing effect of hydrogen bonding between the carbonyl group of one peptide bond and the amino group of another. D) sum of free energies of formation of many weak interactions between its polar amino acids and surrounding water. C) sum of free energies of formation of many weak interactions among the hundreds of amino acids in a protein. B) maximum entropy increase from ionic interactions between the ionized amino acids in a protein. Overview of protein structure Pages: Difficulty: 2 Ans: A The most important contribution to the stability of a conformation appears to be the: A) entropy increase from the decrease in ordered water molecules forming a solvent shell around it. Overview of protein structure Pages: Difficulty: 1 Ans: D All of the following are considered interactions in proteins, except: A) B) C) D) E) hydrogen bonds.

Preview text Chapter 4 The Structure of Proteins Multiple Choice Questions 1.