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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Give 2 structural features in each of the given proteins below that make them perform their biological roles effectively (structural features that directly make them effective in their respective biological roles). Explain how each structural feature directly contributes to proteins’ biological roles.
hemoglobin
immunoglobulin
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Consider protein folding that results when the following components interact:
Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups.
Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.
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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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- All three types of biopolymers are set from the building blocks with similar types of chemical reactions. Draw the chemical reaction formula for the polymerization reaction. Describe two non-covalent interactions that stabilize a tertiary structure of a protein. c.When describing the structure of proteins, it is often done at different levels. Explain what is meant by the following structural levels: primary structure secondary structure tertiary structure quaternary structurearrow_forwardWhich of the following best describes how the secondary structure of a protein is formed? A B с D O=U a-helix H O=C N-H R-C-H C=0 H-N H-C-R O=C N-H R-C-H C=O H-N O-C N-H R-C-H C=O H-N N-H 0= H-C-R H-N C=O R-C-4 N-H O=C H-C-R 4-1 Ç=O R-C-H N-H 0=C H-C-R (=O R-C-H B-pleated sheet ionic bonds between the R groups of the polypeptide amino acids -Uh hydrogen bonds between the carboxyl and amino groups of non-adjacent amino acids covalent bonds between the carboxyl and amino groups of adjacent amino acids hydrogen bonds between the R groups of the polypeptide amino acidsarrow_forwardThe structure shown below belongs to which family of protein tertiary structure? 1) x/B barrel 2) B-barrel 3) x-helix bundle 4) xß-sandwich PDB: 1VRDarrow_forward
- Which statement best describes the protein structure shown below? This is an alpha helix. This is a tertiary structure that consists almost entirely of beta strands. This is a tertiary structure consisting of a roughly equal mixture of alpha helices and beta sheets. This is a beta sheet. This is a tertiary structure that consists almost entirely of alpha helices.arrow_forwardThe structure shown below belongs to which family of protein tertiary structure? PDB: 1Z4A 1) a/ß barrel 2) B-barrel 3) a-helix bundle 4) aß-sandwicharrow_forwardDraw a hydropathy plot and a 2D protein cartoon for a protein that passes through the lipid bilayer 6 times..arrow_forward
- What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.arrow_forwardYou run an SDS-PAGE gel on some purified protein samples against a protein ladder as marked. kDa 225 150 100 75 50 35 25 1) Homodimer with molecular weight of 52 kDa linked by salt-bridges and hydrogen bonds ABCDE 2) Heterodimer with molecular weight of 52 kDa linked by salt-bridges and hydrogen bonds 3) A protein with no quaternary structure that has a molecular weight of 52 kDa B Earrow_forwardWhy should the BRCA1 protein be considered one of the best macromolecules within proteins? Is BRCA1 the best functionally, structurally, or based on other properties? Please explain in detail. You can give examples with scientific articles related to protein.arrow_forward
- Which of the following statements best describe(s) the mechanism by which correct protein folding takes place once the misfolded protein binds the open ring of groEL? Select all that apply. The groEL ring closes to isolate the protein and provide enough time for the protein to properly fold on its own. b and d The groEL ring closes to provide a hydrophilic space to isolate the protein and inhibit its aggregation with others until properly folded. The groEL ring closes to isolate the protein and provide steric hindrance that mechanically refolds the protein. The groEL ring closes to isolate the protein and decode the information necessary to achieve the correct three-dimensional structure. None of the above I picked "The groEL ring closes to provide a hydrophilic space..." but it was incorrect..arrow_forwardGive the force of interaction involved in the protein folding of the protein structure A and C: COO CH,C-N-H• • •0- Pleated sheet structure A H C Helical structure CH3 CH3 - CH3 -CHCH,CH, CH- CH, CH3 (CH,),NH, -0-CCH,- C=0..•HN CH, CH, CH,CH CH,CH CH, CH, CH OH 0=C -CH,-S,S-CH,- H,Ñ Structure A: H-bonding: Structure C: Van der Waals O Structure A: Covalent interaction; Structure C: dipole-dipole interaction O Structure A: Salt bridge: Structure C: H-bonding Structure A: Hydrophobic interaction; Structure C: ionic interaction 00000 Barrow_forwardPage 1 > of 3 ZOOM B. Propose une Toie onsuinin Teguiaung Dioou giucose concentrauon. Question 2: Label the protein structure level on lines 1,2,3, and 4 and label/describe the structure to which each box corresponds. Describe the characteristics of each structural level in the boxes below. MacBook Air DII 80 888 F10 F7 FB F5 F4 F3 * & # $ 7 8 3 4 E R T Y K F M C V .. .. この * 00 Barrow_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