Molec Biochem Chapter 6 Flashcards _ Quizlet

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11/27/23, 9:05 AM Molec Biochem Chapter 6 Flashcards | Quizlet https://quizlet.com/28169216/molec-biochem-chapter-6-flash-cards/ 1/19 Try the fastest way to create flashcards Molec Biochem Chapter 6 12 studiers today 4.7 (3 reviews) Students also viewed Terms in this set (78) Others also viewed these textbooks Search for a textbook or question Organic Chemistry 3rd Edition ISBN: 9781119340577 David Klein 3,098 solutions Protein Structure Part 1 37 terms winterch Preview Chapter 6 Part 2 30 terms ameliadelm Preview Biochem Ch. 5 22 terms Cerina_James Preview proteins 30 terms TheInsan Which one of the following statements about peptide bonds is FALSE. Peptide bonds are: -charged. -covalent. -involved in forming the primary structure of proteins. -amides. -rigid and planar, with partial double-bond character. charged. Which of the following describes the entire three- dimensional structure of a single polypeptide? Tertiary structure Quaternary structure Primary structure Secondary structure Tertiary structure
11/27/23, 9:05 AM Molec Biochem Chapter 6 Flashcards | Quizlet https://quizlet.com/28169216/molec-biochem-chapter-6-flash-cards/ 2/19 Which of the following amino acid residues form hydrogen bonds with Ala residues located in an alpha-helix? -Polar residues involved in the stabilization of tertiary structure. -Residues located within the same -helix. -Residues in a neighbouring -helix. -None, because Ala is unable to form hydrogen bonds. Residues located within the same -helix. A domain is: -a folded segment of polypeptide with -a separate hydrophobic core. -an -helix, β -sheet or irregular secondary structure. -the same as a protein's tertiary structure. -always a motif. a folded segment of polypeptide with -a separate hydrophobic core. Which level of protein structure is defined as "the hydrogen bonded arrangement of the polypeptide backbone"? Which level of protein structure is defined as "the hydrogen bonded arrangement of the polypeptide backbone"? Secondary Tertiary Quaternary Primary Secondary Where are irregular secondary structures (loops) generally found in soluble globular proteins and why? -On the surface so that they can interact with the solvent. -On the surface because they are less compact. -In the core of the protein so that they can interact with hydrophobic groups. -In the core of the protein because they connect β - strands and -helices. On the surface so that they can interact with the solvent. Which of the following statements about quaternary structure is TRUE? -Quaternary structure is defined as the 3D structure of proteins with four subunits. -Quaternary structure requires covalent interactions between polypeptide chains. -Quaternary structure is stabilized by the same types of noncovalent interactions as tertiary structure. -Quaternary structure exists only in proteins containing prosthetic groups. Quaternary structure is stabilized by the same types of noncovalent interactions as tertiary structure.
11/27/23, 9:05 AM Molec Biochem Chapter 6 Flashcards | Quizlet https://quizlet.com/28169216/molec-biochem-chapter-6-flash-cards/ 3/19 Which of the following series of amino acids is most likely to be buried in the center of a water-soluble globular protein? Pro, Gln, His Gly, Asn, Ser Glu, Asp, Lys Ala, Leu, Phe Ala, Leu, Phe Which of the following statements about peptide bonds is FALSE? -Water is released when a peptide bond is formed. -The peptide bond exhibits partial double bond character -The peptide bond has restricted rotation around the bond between the carbonyl carbon and C. -The peptide bond is planar. The peptide bond has restricted rotation around the bond between the carbonyl carbon and C. Which one of the following sequences of five amino acids would most likely be located in the interior of a water soluble globular protein? Tyr-Phe-Glu-Asn-Leu Met-Phe-Pro-Ile-Leu Glu-Asn-Ser-Thr-Gln Val-Ala-Val-Glu-Val Met-Phe-Pro-Ile-Leu Compare the -helix with the structure of double- stranded DNA. Which statement is TRUE for both structures? -The backbones are on the outside of the helix. -The hydrogen bonds are perpendicular to the axis of the helix. -Hydrogen bonds are the primary determinant of stability. -The helices are right handed. The helices are right handed Which one of the following statements about the β - sheet is FALSE? -The side chains in a β -sheet alternate between the two sides of the sheet. -The β -sheet is a type of regular secondary structure. -The β -sheet is a type of secondary structure that fulfills the hydrogen bonding requirements of amino acid side chains. -The β -sheet contains hydrogen bonds between the carbonyl oxygen of one residue and an amide hydrogen of a residue on an adjacent strand. - β -sheets can be parallel or antiparallel. The β -sheet is a type of secondary structure that fulfills the hydrogen bonding requirements of amino acid side chains.
11/27/23, 9:05 AM Molec Biochem Chapter 6 Flashcards | Quizlet https://quizlet.com/28169216/molec-biochem-chapter-6-flash-cards/ 4/19 See an expert-written answer! What ultimately determines the unique three dimensional structure of soluble globular proteins? -The number of subunits. -The exact number of disulfide bonds. -The exact number of H-bonds. -The sequence of the amino acid residues. -The prosthetic groups. The sequence of the amino acid residues. Which of the following sequences of amino acids is most likely to be at the surface of a water-soluble globular protein? Pro-Phe-Thr Ala-Leu-Phe Gly-Tyr-Val Glu-Asp-Lys Ile-Ser-Met Glu-Asp-Lys Which of the following stabilizes the folding of a polypeptide backbone into regular secondary structure? Disulphide bridges. Hydrogen bonds. Covalent bonds. Electrostatic interactions. Hydrophobic interactions. Hydrogen bonds. Which of the following statements about quaternary structure is FALSE? -Quaternary structure is defined as the arrangement of polypeptide backbones in proteins with four subunits -Quaternary structure exists only in proteins containing more than one polypeptide -Quaternary structure is fine-tuned by ion pairs, disulfide bonds, and hydrogen bonds. -Quaternary structure is stabilized primarily by hydrophobic interactions. Quaternary structure is defined as the arrangement of polypeptide backbones in proteins with four subunits Which one of the following statements about the - helix is FALSE? -Side chains are located on the outside of an -helix. -The -helix contains hydrogen bonds between the carbonyl oxygen of one residue and an amide hydrogen that is four residues closer to the carboxy terminus of the helix. -The -helix has a right handed twist. -The -helix is a type of secondary structure that fulfills the hydrogen bonding requirements of amino acid side chains. -The -helix is a type of regular secondary structure. The -helix is a type of secondary structure that fulfills the hydrogen bonding requirements of amino acid side chains.
11/27/23, 9:05 AM Molec Biochem Chapter 6 Flashcards | Quizlet https://quizlet.com/28169216/molec-biochem-chapter-6-flash-cards/ 5/19 Which of the following is TRUE about prosthetic groups? -Prosthetic groups are bound and released by the protein as needed. -Prosthetic groups are an integral part of the three dimensional structure of the protein. -Prosthetic groups are amino acids with additional reactivity. -Prosthetic groups are inorganic. Prosthetic groups are an integral part of the three dimensional structure of the protein Which of the following is FALSE with respect to β - sheets? - β -sheets may be parallel or anti-parallel. -Strands in a β -sheet are connected by irregular loops. - β -sheets are stabilized by non-covalent forces. -Amino acid side chains protrude from one side of the β -sheet. Amino acid side chains protrude from one side of the β -sheet. Which of the following statements about prosthetic groups is INCORRECT? -Heme is an example of a prosthetic group. -Prosthetic groups increase the inherent chemical reactivity of proteins. -Prosthetic groups are not amino acids. -Prosthetic groups form an integral part of the secondary structure of proteins. Prosthetic groups form an integral part of the secondary structure of proteins. Which of the following statements about the -helix and β -sheet are TRUE? 1. They are both types of secondary structure. 2. They are both stabilized by hydrogen bonds between amino acid side chains. 3. The polypeptide backbone is fully extended in both structures. 4. They are both usually located in the interior of soluble globular proteins. 1 and 4 Which of the following statements about the peptide bond is FALSE? -It is a bond that displays resonance. -It is a phosphodiester bond. -It exhibits partial double bond character. -Atoms of the peptide bond are located in a single plane. -It is formed when water is released from the condensation of an amino group and a carboxylic acid. It is a phosphodiester bond.
11/27/23, 9:05 AM Molec Biochem Chapter 6 Flashcards | Quizlet https://quizlet.com/28169216/molec-biochem-chapter-6-flash-cards/ 6/19 Which of the following statements is TRUE regarding the R-groups of amino acid residues in an -helix? -They are found on the exterior of the helix. -They alternate between the outside and the inside of the helix. -They form the hydrogen bonds that produce the helix. -They are found in the interior of the helix. -They cause the helix to be right handed. They are found on the exterior of the helix. Which of the following statements is FALSE? -Both -helices and β -sheets have conformations that minimize steric strain in the polypeptide backbone. -Both -helices and β -sheets have R groups that are oriented away from the core of the structure. -Both -helices and β -sheets form only from adjacent amino acid residues in the polypeptide. -Both -helices and β -sheets are stabilized by hydrogen bonds between groups in the polypeptide backbone Both -helices and β -sheets form only from adjacent amino acid residues in the polypeptide. You have been shown the detailed 3-D structure of an unknown protein. The information indicates that the protein's non-polar amino acid side chains are all exposed on the surface, whereas its polar side chains are all "buried" in the interior. What can you conclude about this protein? -It is likely to be a peripheral membrane protein -It is likely to be a lipid-linked membrane protein. -It is likely to be a soluble cytosolic protein. -It is likely to be an integral membrane protein. It is likely to be an integral membrane protein. Why do Tyr and/or Trp residues tend to destabilize an -helix when they occur next to each other in a protein? -The R group of neither amino acid can form a hydrogen bond. -There is steric hindrance between the bulky Tyr and/or Trp side chains. -There are possible covalent interactions between the Tyr and/or Trp side chains. -Both amino acids are highly hydrophobic. -There is electrostatic repulsion between the Tyr and Trp side chains. There is steric hindrance between the bulky Tyr and/or Trp side chains.
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