Biological Science (6th Edition)
6th Edition
ISBN: 9780321976499
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Emily Taylor, Greg Podgorski, Jeff Carmichael
Publisher: PEARSON
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Chapter 3, Problem 10TYPSS
Make a concept map (see BioSkills 12 ) that relates the four levels of protein structure and shows how they can contribute to the formation of hemoglobin Your map should include the following boxed terms: Primary structure, Secondary structure, Tertiary structure, Quaternary structure, Active site, Amino acid sequence, R-groups, a-Helices.
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Chapter 3 Solutions
Biological Science (6th Edition)
Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - 2. What type of bond is directly involved in the...Ch. 3 - What type of information is used to direct...Ch. 3 - 4. What is an active site?
a. the location in an...Ch. 3 - Prob. 5TYUCh. 3 - Prob. 6TYUCh. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 8TYUCh. 3 - Prob. 9TYPSSCh. 3 - 10. Make a concept map (see BioSkills 12) that...
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- Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.arrow_forwardImagine you were able to incorporate real and artificial amino acids with the following side chains into proteins. Which of these would be most likely to be found on the outside surface of the hemoglobin protein in its folded form at ~pH 7.0? a) -CH2OH b) -phenol (phenyl with -OH) c) -phenyl d) -CH2CH3arrow_forwardWhich of the following statement(s) is/are FALSE for hemoglobin? A Demonstrates positive cooperativity and can bind up to four O2 molecule. B It exhibits the 4 levels of protein structure. C It is a trimer with 2 α-helices and 1 β-sheet. D It is an allosteric protein.arrow_forward
- Linus Pauling’s a-helix structure (found in hemoglobin, myoglobin, actin, myosin, and keratin) is one of the most common examples of which level of protein organization? the quaternary structure the tertiary structure the secondary structure the primary structure all of the abovearrow_forwardAfter denaturation of a tertiary protein like lysozyme (with one polypeptide chain), the only remaining bonds between its monomer subunits will be: the disulfide bonds the van der Waals forces the peptide bonds the hydrogen bonds the ionic bondsarrow_forwardAt what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? Heating a protein (due to fever), causing hydrogen bonds to break. Drastic changes in pH (like the above patients), causing some polar amino acids to turn into non-polar amino acidsarrow_forward
- Which of the following is an example of protein denaturation? * A. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone. B. Several amino acids are joined together together via peptide bonds. C. A protein binds with with a substrate, lowering the activation energy of reaction. D. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be left with only its primary structure. E. Results to unfolding, partial or incomplete disorganization of the protein's secondary and tertiary structure.arrow_forwardWhich 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 interactionsarrow_forwardDiscuss the different structures (primary, secondary, tertiary, and Quaternary structures) of protein. What are the five factors that promote protein folding and stability. (Hint: One factor is the Hydrogen bond). Extra Hint: Another factor is the Hydrophobic effect.arrow_forward
- What is the primary driver of protein folding on a macro level? a. Hydrogen bonding b. Van der Waals forces c. Covalent bonding d. Entropic forcearrow_forwardWhat is Protein folding? Give at least 3 diseases that results from protein misfolding. Explain each. Can you give me a brief explanation about this question? Not less than 3 sentences.arrow_forwardThe amino sequence of a protein is: alanine, leucine, valine, threonine. This information reveals the protein’s _______ structure. The “C” terminus or side of this protein is ______. Select one: a. primary, alanine b. secondary, alanine c. secondary, leucine d. secondary, threonine e. primary, threoninearrow_forward
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