Biological Science (7th Edition)
7th Edition
ISBN: 9780134678320
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Greg Podgorski, Emily Taylor, Jeff Carmichael
Publisher: PEARSON
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Chapter 3, Problem 9TYPSS
Summary Introduction
To review:
Based on information about the peptide bonds that link together amino acid residues, the reason behind side chain containing proline reduced the flexibility of the backbone.
Introduction:
Proline is the amino acid where the alpha-amino group is attached directly to the side chain, making the alpha carbon a direct substituent of the side chain.
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Amino acids have the generic structure, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.
Chapter 3 Solutions
Biological Science (7th Edition)
Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - What type of information is used to direct...Ch. 3 - Prob. 5TYUCh. 3 - Prob. 6TYUCh. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 9TYPSSCh. 3 - Prob. 12PIATCh. 3 - Prob. 13PIATCh. 3 - Recall that proline often introduces kinks in the...Ch. 3 - SOCIETY Based on the experiment in question 15,...
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- What type of noncovalent interaction occurs between the glutamine and threonine side chains? Draw the structures of these amino acids to show the interaction.arrow_forwardOn a sheet of paper , sketch a picture of a dehydration synthesis reaction between two amino acids. This is not meant to be tricky! Use Fig. 3.18 as a model. Be sure to identify what specific atoms on each amino acid will be involved in the reaction, and be sure and show the solid line that denotes the new covalent bond that will exist in the product. On one of your amino acids, label the amino group, the carboxyl group, and the side chain. FInally, point to and label the peptide bond in the resulting dipeptide. Take a picture of your lovely drawing and upload it here.arrow_forwardOn a sheet of paper , sketch a picture of a dehydration synthesis reaction between two amino acids. This is not meant to be tricky! Use Fig. 3.18 as a model. Be sure to identify what specific atoms on each amino acid will be involved in the reaction, and be sure and show the solid line that denotes the new covalent bond that will exist in the product. On one of your amino acids, label the amino group, the carboxyl group, and the side chain. FInally, point to and label the peptide bond in the resulting dipeptide. Take a picture of your lovely drawing and upload it here.arrow_forward
- What is the advantage of having an amino acid that’s hydrophobic? Please explain using an example.arrow_forwardDraw the following amino acids interactions: 1. H-bond - between -0H of Serine amino acid and C=0 backbone of glutamic acid. 2. Ionic bond- between ionized aspartic and asparagine amino acids. 3. Disulfide interaction between 2 molecules of Cysteine amino acids. 4. Hydrophobic interaction between Alanine and Leucine R-groups.arrow_forwardDraw the peptide ASK(ala-ser-lysine) with proper stereochemistry? what is its pI(isoelectric point)and why the structure is planar? Use the following table to look at pka's of the amino acids and solve this question.arrow_forward
- How does the structure of chymotrypsin enable it to cleave only peptide bonds that are adjacent to aromatic R groups? Suppose a protease could only cleave adjacent to Lysine and Arginine; how would the structure of this protein differ from that of chymotrypsin?arrow_forwardDraw the two amino acids serine and alanine, and a dipeptide that could be formed by combining these two amino acids (ala-ser). Draw these molecules at a pH=7. In peptide nomenclature the amino terminus is on the left and the carboxyl terminus is on the right. 1. How many waters were released by formation of this dipeptide from individual amino acids? [ Select ] 2. How many hydrogen bond donors does your dipeptide have? [ Select ] 3. If you were to draw this dipeptide at a pH :1, would the number of hydrogen bond donors change? [ Select ]arrow_forwardIn N-linked glycoproteins, the sugar is usually attached to the protein by a bond to the N atom in a side-chain amide. Which amino acids can form such a bond?arrow_forward
- What is wrong about calculating charge of a polypeptide based on the pKa of individual amino acids? In other words, what can happen to pKa when amino acids are brought together in a polypeptide chain?arrow_forwardShown below are three amino acids: H,N-CH-C-o ҫн, H,N-CH-C-o CH, H,N-CH-C-o ČH, Tyrosine Tyr Y Phenylalanine Phe F Alanine Ala A 1. Which amino acid is the least hydrophobic? 2. Which amino acid is most hydrophobic? 3. Which amino acid is intermediate? 4. Explain why (2) is more hydrophobic than (3). 5. Explain why (3) is more hydrophobic than (1).arrow_forward(iii) Draw a structural diagram of a hydrogen bond between β-D-glucose and the side chain of any polar residue in a protein. (iv) Name the type of bond that can occur between the axial hydrogens of glucose and the indole ring of tryptophan. Draw a structural diagram of this bond. (v) Comment on the polar / apolar nature of the bond in part (iv) and explain why this type of interaction is prevalent in protein-sugar complexes. Answer (iii) to (v) please.arrow_forward
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