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 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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Explain why amino acid can increase blood glucose.
Write the structure of each of the following peptide at pH7 and identify how many peptide bond in each number.
Alanyl-phenylalanine- aspartate- cysteine
Threonyl- Isoleucyl-methionyl- leucine
Lysyl-alanine -Phenylalanyl-tyrosyl- serine
Compare and contrast the biological roles of the following amino acids the following pairs ofamino acids. Once you have documented these role state which member of the pair is most important and why.
What is the advantage of having an amino acid that’s hydrophobic? Please explain using an example.
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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- At what pH does Aspartate have a net charge of -1 (negative 1)? For Aspartate, the pKa of the alpha carboxylate is 1.88, the pKa of the side-chain carboxylate is 3.65, and the pKa of the alpha amino group is 9.60 Show how you calculate your answer.arrow_forwardSome bacteria produce poly-γ-glutamic acid, a polymer in which the amino group of each glutamate residue is condensed with the γ-carboxylate group of the adjacent residue. Draw the repeating structure of this polymer.arrow_forwardWhat type of noncovalent interaction occurs between the glutamine and threonine side chains? Draw the structures of these amino acids to show the interaction.arrow_forward
- Draw 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_forwardImagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. In the table below are four possibilities for what R, and R, might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ R₂ threonine cysteine glutamine arginine cysteine tyrosine phenylalanine glutamate specific interaction? Oyes no yes O no O yes O no Oyes O no name of specific interaction 0 0 0 0 Xarrow_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_forward
- Which functional group(s) shown above is (are) present in all amino acids?arrow_forwardHow 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_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
- Draw the structure of the a-keto acid formed by the transamination of each amino acid: (a) tyrosine (b) asparagine draw structure ... draw structure ***arrow_forwardWhat 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_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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