Concept explainers
(a)
Interpretation:
Level of protein structure determined by peptide bond between the amino acid is to be identified.
Concept introduction:
Level of Protein structure,
- Primary structure
- Secondary structure
- Tertiary structure
- Quaternary structure
Primary structure is the sequence of amino acid connected by peptide bond in a polypeptide chain.
(b)
Interpretation:
Level of protein structure determined by hydrogen bonds is to be identified.
Concept introduction:
Secondary structure is the arrangement of polypeptide chain, in a regular pattern of
(c)
Interpretation:
Level of protein structure determined by R group interaction is to be identified.
Concept introduction:
Tertiary structure is the folding of a single protein into a specific three dimensional shape, held by noncovalent interaction between the side chains.
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Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
- Describe the four levels of protein structure. How do a proteins side groups influence its interactions with other substances? What happens when a protein is denatured?arrow_forwardHow do the following noncovalent interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could giverise to each interaction.(a) Hydrophobic interactions(b) Salt bridges (ionic interactions)arrow_forwardWhich of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (B) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (E) They require a high content of proline and glycinearrow_forward
- How do the following interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.(a) Side-chain hydrogen bonding(b) Disulfide bondsarrow_forwardWhich of the following statements is true about the quaternary structure of a protein? A) The quaternary structure of a protein is based on how polypeptide subunits interact with one another. B) The quaternary structure of a protein is affected by hydrogen bonds. C) The quaternary structure is the overall shape of a protein. D) The quaternary structure is driven by a- helices and B-pleated sheets. E) The quaternary structure is found in all proteins.arrow_forwardWhich of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (8) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (€) They require a high content of proline and glycinearrow_forward
- In a subunit of a protein, arginine and aspartic acid have an ionic interaction between their side chains. Part a) If arginine is changed to glutamic acid, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part b) If arginine is changed to lysine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part c) If arginine is changed to isoleucine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why.arrow_forwardIdentify the following statements as descriptive of the secondary, tertiary, or quaternary structure of a protein. What types of interactions stabilize each type of structure?(a) The polypeptide chain has a number of bends and twists, resulting in a compact structure.(b) The polypeptide backbone forms a right-handed coil.(c) The four polypeptide chains are arranged in a spherical shape.arrow_forward(a) Are all proteins polymers? What is the basie unit of protein? Explain the formation of Zwitterion in a-amino acid. (b) Count the number of peptide bonds in the below structure. -R-N-C-R-N-C-R-N-C-R-N-C- wwww H H H Harrow_forward
- Amino acid structure and composition: Assuming physiological pH conditions, draw the peptide backbone of a protein composed of four amino acids. The protein is a) overall positively charged b) capable of forming disulfide bond with another protein c) has two amino acid that can participate in hydrogen bond formation d) one peptide bond in cis conformation you must show the complete name, single letter abbreviation and structure of each amino acid. Make sure to highlight the peptide bond that is in cis conformationarrow_forwardProper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structurearrow_forwardProtein denaturation usually refers to the disruption of which of the following types of molecular interactions? Select all that apply. A.)Van der Waals attraction B.)Covalent bonds C.)Hydrogen bonds D.)Hydrophobic interactionsarrow_forward
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