Essentials of Human Anatomy and Physiology (Custom)
15th Edition
ISBN: 9781269752862
Author: Marieb
Publisher: PEARSON
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Chapter 2, Problem 9MC
Summary Introduction
Introduction:
The protein is a
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Describe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)
Which of the following statements are correct about the native state of a protein (select all that apply)?
A.
Polar sidechains commonly interact with water
B.
Hydrophobic amino acids tend to be on surface of protein
C.
The sidechains of polar amino acids are most commonly found in the central core of a protein
D.
Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains.
E.
Secondary structure is largely driven by hydrophobic interactions
Which of the following is incorrect concerning protein structure
determination by X-ray crystallography?
Choose one:
O A. X-ray crystallography provides dynamic information
about protein structure.
O B. A 1.5 Å resolution structure is better than a 3 Å
resolution structure.
O C. Isomorphous replacement is used to aid phase
determination.
O D. Highly ordered crystals are required.
Chapter 2 Solutions
Essentials of Human Anatomy and Physiology (Custom)
Ch. 2 - Prob. 1MCCh. 2 - Prob. 2MCCh. 2 - Prob. 3MCCh. 2 - Prob. 4MCCh. 2 - Glucose is to starch as a. a steroid is to a...Ch. 2 - 6. What lipid type is stored in fat deposits...Ch. 2 - Absence of which of the following...Ch. 2 - ATP is not associated with a. a basic nucleotide...Ch. 2 - Prob. 9MCCh. 2 - 10. Factors that increase the speed of chemical...
Ch. 2 - Why is a study of basic chemistry essential to...Ch. 2 - Matter occupies space and has mass. Explain how...Ch. 2 - Prob. 13SAECh. 2 - Prob. 14SAECh. 2 - Prob. 15SAECh. 2 - Prob. 16SAECh. 2 - All atoms are neutral. Explain the basis of this...Ch. 2 - Fill in the following table to fully describe an...Ch. 2 - Define radioactivity. If an element has three...Ch. 2 - Prob. 20SAECh. 2 - Prob. 21SAECh. 2 - Where would you expect to Find hydrogen bonds in...Ch. 2 - The two oxygen atoms forming molecules of oxygen...Ch. 2 - Prob. 24SAECh. 2 - 25. Identify each of the following reactions as a...Ch. 2 - Prob. 26SAECh. 2 - Prob. 27SAECh. 2 - 28. Define pH. The pH range of blood is from 7.35...Ch. 2 - Prob. 29SAECh. 2 - Prob. 30SAECh. 2 - Describe the structural differences between...Ch. 2 - Prob. 32SAECh. 2 - 33. Name the two protein classes based on...Ch. 2 - Prob. 34SAECh. 2 - Describe what has happened to a proteins structure...Ch. 2 - Prob. 36SAECh. 2 - Prob. 37SAECh. 2 - 38. Explain why you can “stack” water slightly...Ch. 2 - Explain what is meant by the terms synthesis...Ch. 2 - 41. Several antibiotics act by binding to certain...Ch. 2 - 42. Mrs. Roberts, who is in a diabetic coma, has...Ch. 2 - Tendons, ligaments, and skin contain a large...Ch. 2 - Prob. 43CAQ
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- Which of the following statements are correct about protein structure (select all that apply)? A. Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein B. Only amino acids with a net charge may interact with other amino acids C. The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role. D. Hydrophobic interactions play a key role in protein folding E. Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acidsarrow_forwardBiochemists talk about protein structure at four distinct levels: primary, secondary, tertiary and quaternary structure. Below are depictions of each of these levels of protein structure. For each image, match the term and the written description of the level of protein structure that the image depicts. Drag the appropriate items to their respective bins.arrow_forwardA protein in its native three dimensional conformation is cleaved with trypsin. According to the amino acid sequence, there are 9 residues where trypsin could cleave, yet only 3 fragments were produced from the digest. What conclusion can be made about protein structure that would lead to this result? The protein has multiple domains b. The protein is highly compacted, minimally accessible by solvent molecules c. The protein has quaternary structure d. The protein has a dynamic structure, highly accessible by solvent molecules e. The protein is compromised only of alpha helicesarrow_forward
- Match the description of each structural level of proteins on the left with the appropriate a, the three-dimensional shape of a complete polypeptide Tertiary structure b. the order of amino acids found in a polypeptide Primary structure c. the attachment of multiple polypeptides Quaternary structure together d. pre-defined shapes that exist as part of a larger polypeptide Secondary structure c) Jean-François is studying a specific protein in a research laboratory. In previous experin he observed that this protein seems to function as a receptor protein on the surface of cells recognizes a specific hormone involved in cell-cell communication. Jean-François prepares his final experiment, but makes a mistake in calculating how mucl add to one of his solutions to get the correct pH. He performs the experiment, and much te surprise, he observes that his protein no longer seems to be recognizing the hormone anyr he had observed in previous experiments. Propose a hypothesis that briefly…arrow_forward3. 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?arrow_forwarda.Describe the bonds which hold a quaternary protein molecule together. b. Discuss the reasons why glycine and proline are not usually found in an alpha helix of proteins.arrow_forward
- Oftentimes, the major challenge in the determination of protein structure via X-ray crystallography is the production of good crystals. One common approach is to crystallize fragments of the whole protein instead of crystallizing the whole protein. If you were to cleave a protein into fragments that will still retain the folding of that fragment in the whole protein, where is the best location to perform the cleavage? O At the ends of each alpha helix. O At the ends of a protein motif. O At the points connecting protein domains. O At the ends of beta strands.arrow_forwarda. Classify tertiary structures of proteins and give one example from each class. b. In their tertiary structures some proteins are known to fold into specific nativa conformations. Discuss protein folding and the forces stabilizing them. A Paragraph В I 国 回arrow_forwardPhysical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryo electron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?arrow_forward
- Indicate the level(s) of protein structure to which each of the following contributes: a. amino acid sequence b. β-pleated sheet c. hydrogen bond d. disulfide bondarrow_forwardWhich 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.arrow_forwardThe primary structure of a protein is shown below. Please answer the following questions. Leu-Arg-Ser-lle-Glu-Thr-Val-Val-Asn-Gln-Val-lle-Ser- Tyr a. Where is this section of the polypeptide most likely located [ Select ] completely embedded inside the protein partially exposed to the aqueous environment b. Is the above more likely an alpha helix or a beta-pleated sh completely exposed to the aqueous environment c. Which two amino acid residues are least likely to be in an alpha helix, but most likely to be a part of a beta turn? (Please select the amino acids in alphabetical order). [ Select ] [ Select ]arrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY