The structures of the amino acids leucine and isoleucine are shown:H0OH HCH,CHH₂C CH₂LeucineCHH₂COHCH₂CH₂Isoleucinea. Explain how the structure of amino acids determine the function.b. A mutation occurred in DNA of a globular enzyme. If the leucine amino acids were found within the active site of the enzyme, describe the effect this change is likely to have on enzymatic function.c. If a mutation in the DNA of a globular enzyme changed all of the leucine amino acids to isoleucine, predict how the relative position of the amino acid in the tertiary structure of the protein would be affected whenthe protein is placed in an aqueous solution.d. Justify your prediction by providing evidence that supports your claim.

A protein's function depends on its structure. There are four levels of protein structure: primary,…

Answered: The structures of the amino acids…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The structures of the amino acids lysine and aspartic acid are shown: H₂ H OH CH₂ CH₂ CH₂ CH₂ NH₂ Lysine H H H N-C-C CH₂ C OH O НО Aspartic Acid The tertiary structure of a given protein contains an interaction between aspartic acid and lysine. a. Explain how the structure of amino acids determine the function. b. A mutation occurred in DNA of a globular enzyme. If the lysine amino acids were found within the active site of the enzyme, describe the effect this change is likely to have on enzymatic function. c. If a mutation in the DNA of a globular enzyme changed all of the lysine amino acids to aspartic acid, predict how the relative position of the amino acid in the tertiary structure of the protein would be affected when the protein is placed in an aqueous solution. d. Justify your prediction by providing evidence that supports your claim.
Modern medicine now uses insulin analogues (where one or more of the amino acid residues has been changed) in the treatment of diabetes. In one such analogue, glargine insulin, the changes have increased the isoelectric point of the enzyme from 5.4 to 6.7, thereby reducing its solubility at physiological pH. Explain how changes in the primary amino acid sequence can alter the pI and solubility of the analogue without altering its interaction with blood glucose.
Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln 8. How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. 9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. 12. Cyanogen bromide is a chemical reagent which also cleaves peptide bonds.…
Bovine insulin is composed of two polypeptide chains that are linked together covalently. The two chains have the following sequences: GIVEQCCASVCSLYQLENYCN - A chain FVNQHLCGSHLVEALYLVCGERGFFYTPKA - B chain a. Through which amino acids are these two chains linked together covalently? b. How many different ways can these two chains be linked? c. Of the different connectivities you enumerated in part b, which is the biologically active form?
Compare the DNA Sequence and any DNA base that is different in the cow and human sequences. How many bases are different? Examine the amino acids produced. any amino acids that are different in the two sequences. How many are there? What if a mutation occurred in the human insulin gene and the first triplet was changed to C C G? Is this a substitution mutation? Explain how you know. Determine the amino acid chain coded for by the following sequence. Suppose a mutation occurs where another A is added after the first codon. What would the new sequence of amino acids be? How many are there?
Show the peptides that would result from cleavage by the indicated reagent: a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsin
The endorphins are a group of naturally occurring neurotransmitters that act in a manner like morphine to control pain. Research has shown that the biologically active parts of the endorphin molecules are simple pentapeptides called enkephalins. Draw the structure of the methionine enkephalin with the sequence Tyr-Gly-Gly-Phe-Met. Identify the N-terminal and C-terminal amino acids. Bradykinin is a nonapeptide that stimulates smooth muscle contraction, dilates blood vessels, causes pain, and is a component of bee venom. Give the IUPAC name of the nonapeptide. Note: The selected photo is the sequence of Bradykinin.
Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. List down the different fragments that would result if dynorphin were cleaved by trypsin. . How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. . Cyanogen bromide is a chemical reagent which also cleaves peptide bonds. What is/are…
Imagine 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 X
Two peptide sequences are shown below.Peptide A: N-term – GDL – C-termPeptide B: N-term – GTL – C-terma. Draw each peptide at physiological pH. Circle each ionizable functional group in your drawing.b. Briefly explain why changing aspartate to threonine changes the number of ionizable functionalgroups in the peptide chain.c. Briefly explain why the functional group found in aspartate’s side chain is ionizable but the functionalgroup found in threonine’s side chain is not.
An enzyme that catalyzes disulfide– sulfhydryl exchange reactions, called protein disulfide isomerase (PDI), has been isolated. PDI rapidly converts inactive scrambled ribonuclease into enzymatically active ribonuclease. In contrast, insulin is rapidly inactivated by PDI. What does this important observation imply about the relation between the amino acid sequence of insulin and its threedimensional structure?
Draw the structure of the a-keto acid formed by the transamination of each amino acid: (a) tyrosine (b) asparagine draw structure ... draw structure ***

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