52. Which of the following statements are TRUE? |- A peptide bond joins the free carboxyl terminal end of an amino acid with the N-terminal end of another. II - A telephone cord's spiral shape is synonymous to the secondary level of a protein's structure. III - Assisting in the molecular folding of polypeptide chains is one of the essential functions of molecular chaperones. IV - A supercoiled structure describes the tertiary level of a protein chain. A. I only В. 1, II C. I, II, III D. I, II, III, IV 53. What hierarchical structure of a protein is being shown in the illustration below? A. Primary B. Secondary C. Tertiary D. Quaternary + NH CH NH CH CH NH. CH R3

52. Which of the following statements are TRUE? |- A peptide bond joins the free carboxyl terminal end of an amino acid with the N-terminal end of another. II - A telephone cord's spiral shape is synonymous to the secondary level of a protein's structure. III - Assisting in the molecular folding of polypeptide chains is one of the essential functions of molecular chaperones. IV - A supercoiled structure describes the tertiary level of a protein chain. A. I only В. 1, II C. I, II, III D. I, II, III, IV 53. What hierarchical structure of a protein is being shown in the illustration below? A. Primary B. Secondary C. Tertiary D. Quaternary + NH CH NH CH CH NH. CH R3

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 19QP: Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the...

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15,2
A biochemist is designing a peptide that will form the most stable α-helix possible. He needs to synthesize an α-helix to contain a polar surface and a nonpolar surface. Assume the peptide sequence is as follows, where the numbers represent each individual amino acid in the chain. 1 – 2 – 3 – 4 – 5 – 6 – 7 – 8 – 9 – 10 – 11 – 12 The biochemist asks for your assistance. Propose a peptide sequence that would best satisfy the criteria above by providing the amino acid identity at each position (#1-12: i.e. 1-Glycine – 2-proline – 3-glycine – 4-tryptophan....). Briefly explain your design strategy by describing why the amino acids you chose are appropriate for each position (10 sentences). Make sure to include information on α-helix stability and its chemical characteristics with the properties of each amino acid chosen.
Name two(2) interactions that maintain tertiary protein structure.
43.
3) In his haste to create the chapter 2 homework assignment, the biochemistry professor quickly drew the structure of the polypeptide segment Ala-Lys-Thr within a larger, naturally-occurring protein chain at pH 7.4 Can you spot three mistakes the professor made? H3 G 'N H H H₂N H H HO ||/.. H CH3 Mistakes: 1. 2. 3.
3. A. Briefly discuss the four levels of structure in proteins. Knowing that the 3-dimensional shape of a protein is important to its function, discuss on a qualitative basis whether the changes below will likely alter the function of a protein, justifying your answer with why or why not. B. What would happen to a protein's functionality if a serine residue were replaced with threonine? C. What would happen if serine were replaced with leucine? D. What would happen if serine were replaced with cysteine? E. What would happen if aspartic acid were replaced with tryptophan in the part of the protein (an enzyme) that serves as an active site to catalyze a reaction? F. What would happen if aspartic acid were replaced with tryptophan in a non-active site?
1. What are the effects of a) amino acid composition and sequence and b) intramolecular and intermolecular forces of attraction to protein folding? 2. What molecular property of amino acids can be used to justity the concept that the "molecular part of the protein can exhibit the same property as the molecular 'whole' (protein molecule?). Provide a comprehensive discussion using one molecular property. 3. Discuss two metabolic disorders which are caused by protein misfolding. Explain the metabolic consequence of the disorder. 4. If a non-science person asks you what protein folding is and how the concept is related to metabolic disorders, how are you going to explain the concept? (please summarize the concepts used, thank you!)
3a) Secondary (2°) structure in proteins refers to two specific conformations a region of a protein can take on, the a-helix and the b-pleated sheet. Briefly describe or explain how 2° structure forms/what causes 2° structure to form in a region of a protein.
1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric point of the amino acids are as follows; histidine 7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
Which of the following is incorrect? (₁) a. A heterodimer is composed by two identical polypeptide chains b. The polypeptide chains in a multimeric protein are called subunits A homotrimer can be represented with the Greek letter alpha with a sub-index 3 d. Monomeric proteins do not have quaternary structure c.
Regarding the last answer choice, how come both alpha helices and beta sheets aren't denatured when the heat breaks peptide bonds? If heat were to break peptide bonds, wouldn't that affect the primary structure which inevitably affects the more complicated structures?
8) The figure shows an unfolded polypeptide consisting of six amino acids. Describe how cooperativity will drive protein folding of the polypeptide chain into an alpha-helixe- 10EEHOW is AG changed as each amino acid is incorporated into the secondary structure - s)? O H O H 3 H. H. 5 CH-C H. 6 -N-CH-C- OH O H,N CH-C -N CH C-N CH CH CH2 CH2 CH2 CH2 CH OH CH H;C CH3