Bovine insulin is composed of two polypeptide chains that are linkedtogether covalently. The two chains have the following sequences:GIVEQCCASVCSLYQLENYCN - A chainFVNQHLCGSHLVEALYLVCGERGFFYTPKA - B chaina. Through which amino acids are these two chains linked togethercovalently?b. How many different ways can these two chains be linked?c. Of the different connectivities you enumerated in part b, which isthe biologically active form?

The peptide hormone known as insulin is generated by the beta cells of the pancreatic islets and is…

Answered: Bovine insulin is composed of two…

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 enzyme hexokinase adds a phosphate toD-glucose but ignores its mirror image, L-glucose. Supposethat you were able to synthesize hexokinase entirely fromD-amino acids, which are the mirror image of the normalL-amino acids.A. Assuming that the “D” enzyme would fold to a sta-ble conformation, what relationship would you expect it tobear to the normal “L” enzyme?B. Do you suppose the “D” enzyme would add aphosphate to L-glucose, and ignore D-glucose?
Draw the structure of the a-keto acid formed by the transamination of each amino acid: (a) tyrosine (b) asparagine draw structure ... draw structure ***
Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?
The structures of the amino acids leucine and isoleucine are shown: H 0 OH H CH, CH H₂C CH₂ Leucine CH H₂C OH CH₂ CH₂ Isoleucine a. 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 when the protein is placed in an aqueous solution. d. Justify your prediction by providing evidence that supports your claim.
. The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme C would result in exces- sive urinary excretion of what compound?
In relation to the peptide sequence that is presented. -Gly - Ser – Cys – Asp – Glu – Arg – Cys – Arg- ................ S_____________________S The correct option is A. Contains more negative than positive residues B. Contains only one charged alpha-aa C. The formation of the disulfide bridge is incorrect D. Hydrophilic and charged residues predominate
A small protein has a sequence ACNCKAAPMLCARYCAMLH. The structure of this single peptide is stabilized by the formation of two separate disulfide bonds, but the locations of those disulfide bonds are unknown. In order to determine the location, you purify this peptide and treat it with trypsin (cleaves peptide bond at long, positively-charged side chains). Tryptic digestion generated two peptides. Based on this result, determine the location of the –S-S– bonds. Show them in a diagram on the sequence by connecting the corresponding residues. Explain your reasoning.
If both cysteine residues on the B chain of insulin were changes to alanine residues, how would it affect the quaternary structure of insulin?
H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14
Amino acid sequence in a protein that can form N-glycosylation is called a glycosylation sequon. Which of the following is such a sequon? a. Asn-Ala-Thr b. Gln-Ala-Thr c. Asn-Pro-Pro d. Asn-Ala-Ala e. Gln-Ala-Ala
Draw the structure of the α-keto acid formed by the transamination of each amino acid: (a) tyrosine; (b) asparagine.
Patients suffering from sickle cell anemia have a mutation in the gene that codes for one of the hemoglobin chains, in which a single glutamate is replaced by a valine. Propose an explanation for why this substitution has such a striking effect on protein structure and function with explanation. Suggest two other amino acids that would be less likely to cause such serious impairment of hemoglobin function if each was substituted for glutamate. Briefly explain your answer.

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