Essentials of Genetics (9th Edition) - Standalone book
9th Edition
ISBN: 9780134047799
Author: William S. Klug, Michael R. Cummings, Charlotte A. Spencer, Michael A. Palladino
Publisher: PEARSON
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Chapter 12, Problem 11PDQ
Refer to Table 12.1. Can you hypothesize why a mixture of (Poly U) + (Poly A) would not stimulate incorporation of 14C-phenylalanine into protein?
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Determine the sequence of the following 10-mer of ferritin using the data below. i. Complete acid hydrolysis of the 10-mer results in identification of 1A, 1D, 1E, 1F, 1H, 1K, 2L, 1T, 1Y ii. Digestion of the 10-mer with chymotrypsin results in 3 fragments containing (D, H, K, T), (F, L) and (A, E, L, Y) iii. Digestion of the 10-mer with V8 protease, which cuts on the C-side of acidic amino acids, results in three fragments containing (D, F, L, Y), (A, E, L) and (H, K, T) iv. Digestion with trypsin results in a fragment H-T and a fragment with all the other amino acids v. Treatment of the 10-mer with FDNB followed by complete acid hydrolysis results in the following two derivatives, DNP-1 and DNP-2 vi. Treatment of the 10-mer with a carboxypeptidase results in a free threonine
You have isolated from a rare fungus an octapeptide that prevents baldness and you wish to determine its amino acid sequence. The amino acid composition is K2, D, Y, F, G, S, A. Reaction of the intact peptide with dansyl chloride yields dansyl-A. Cleavage with trypsin yields peptides whose compositions are: (K, A, S) and (G, F, K) plus a dipeptide. Reaction with chymotrypsin releases free D, a tetrapeptide with composition (k, S, F, A) and a tripeptide whose composition following acid hydrolysis is (G, K, Y). The enzymatic digests are each carried out on the whole, undansylated peptide.What is the sequence?
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Chapter 12 Solutions
Essentials of Genetics (9th Edition) - Standalone book
Ch. 12 - CASE STUDY | A drug that sometimes works A...Ch. 12 -
CASE STUDY | A drug that sometimes works
A...Ch. 12 -
CASE STUDY | A drug that sometimes works
A...Ch. 12 - HOW DO WE KNOW? In this chapter, we focused on the...Ch. 12 - Review the Chapter Concepts list on p. 215. These...Ch. 12 - In studies of frameshift mutations, Crick,...Ch. 12 -
4. The mRNA formed from the repeating...Ch. 12 - In studies using repeating copolymers, AC......Ch. 12 - Prob. 6PDQCh. 12 - Prob. 7PDQ
Ch. 12 -
8. When the amino acid sequences of insulin...Ch. 12 - Prob. 9PDQCh. 12 - Why doesn't polynucleotide phosphorylase (Ochoa's...Ch. 12 - Refer to Table 12.1. Can you hypothesize why a...Ch. 12 -
12. Predict the amino acid sequence produced...Ch. 12 - A short RNA molecule was isolated that...Ch. 12 - A glycine residue exists at position 210 of the...Ch. 12 - Shown here is a theoretical viral mRNA sequence...Ch. 12 -
16. Most proteins have more leucine than...Ch. 12 - Define the process of transcription. Where does...Ch. 12 - Describe the structure of RNA polymerase in...Ch. 12 - In a written paragraph, describe the abbreviated...Ch. 12 - Messenger RNA molecules are very difficult to...Ch. 12 - One form of posttranscriptional modification of...Ch. 12 - In a mixed copolymer experiment, messages were...Ch. 12 -
23. Shown in this problem are the amino acid...Ch. 12 - Alternative splicing is a common mechanism for...Ch. 12 - The genetic code is degenerate. Amino acids are...
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- An octapeptide was hydrolyzed and the amino acids separated. Its amino acid composition was determined: Gly (1); Ala (2); Val (1); Lys (2); Met (1); Asp (1). After incubation with FDNB and hydrolysis, 2,4-dinitrophenylalanine was detected. NO2 H H N C COOH ON- CH, Treatment with cyanogen bromide, which cleaves at M, resulted in two fragments: a pentapeptide containing two K residues and a tripeptide containing V, G, and A. The residues are not listed in any particular order. After treatment with trypsin, which cleaves at R and K, there were three fragments: two dipeptides and MGAV. What is the sequence of the octapeptide? Use the one-letter abbreviations for the amino acids, and do not use dashes.arrow_forwardSelect the term in column B which best matches the description in column A. There are more terms then needed. Column A Column B 1. The pentose sugar found in DNA. a) Cis fatty acid b) Trans fatty acid c) Coenzyme d) Cofacipr 2. Commonly referred to as "insoluble fiber". 3. Considered to be an amphipathic molecule. 4. A molecule with the formula C18H3602 is probably a e) Phospholipid 5. Bond created during the formation of the primary structure of a protein. ) Glycogen 6. A non-protein organic molecule needed for proper enzyme functioning. g) Cellulose 7. Pyrimidine base found only in RNA. h) Galactose i) Fructose 8. Increasing the number of these molecules in the cell membrane would increase the permeability of the cell membrane. i) Thymine k) Uracil 9. Bond which connects nucleotide monomers together. 1) Fatty acid m) Disaccharide n) Peptide bond o) A-Helix p) B-Pleated Sheet q) Ribose r) Deoxyribose 10.arrow_forwardA peptide with endorphin-like property was produced and obtained from the blood. This was sequence using the protocol: Treatment with streptococcal protease gave a tripeptide and a tetrapeptide. Treatment with trypsin gave two tripeptides and an amino acid. Treatment of the 2 tripeptide products in 1.2 with 2,4-dinitrophenol gave DNP- S, and DNP-E and a mixture of amino acids. The composition of the peptide is G, E, S, and K in a 2:1:1:3 molar ratio. a. Determine the sequence of the peptide? b. Determine the pl and position in an electrophoretic profilearrow_forward
- A peptide with endorphin-like property was produced and obtained from the blood. This was sequence using the protocol: Treatment with streptococcal protease gave a tripeptide and a tetrapeptide. Treatment with trypsin gave two tripeptides and an amino acid. Treatment of the 2 tripeptide products in 1.2 with 2,4-dinitrophenol gave DNP- S, and DNP-E and a mixture of amino acids. The composition of the peptide is G, E, S, and K in a 2:1:1:3 molar ratio. What is the sequence of the peptide?arrow_forwardA) Draw the "standard" base pairs (A:T and G:C) but instead of using the most common form of each base, use the uncommon tautomer form of each base (i.e. imino A, imino C, enol G, enol T). Clearly indicate hydrogen bonds (an arrow from donor to acceptor will suffice). Be sure to include the “R” representing the pentose. B) The G:U "wobble" base pair can be formed between the most common tautomer forms of G & U. Another base pair with the same geometry/pairing/orientation can be formed between G & T. Can you create a "wobble" base pair between the uncommon enol tautomer forms of G & T? Like the "wobble" G:U base pair in the Lecture 1 slides, this enol-based "wobble" G:T base pair must have at least two hydrogen bonds. If possible, draw such a base pair, and note any important differences from the non-enol G:U/T wobble. If it is not possible to draw such a base pair, explain why.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_forward
- There is parts A-D for the picture provided. A) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 1? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 B) A peptide has the sequence Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 5? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 C) Same Peptide sequence, What is the net charge at pH8.5, (N-terminus is pronated) Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 D) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 13? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 Thank You!arrow_forwardDraw the complete structure of the tetrapeptide Val-Cys-Glu-Ser.arrow_forwardCan the same pepptide be used in multiple different proteins? yes or no, explain.arrow_forward
- A picture of the two disaccharide repeats of hyaluronic acid are shown below. Name the two different glycosidic linkages. Are these the same linkages as those found in glycogen?arrow_forwardA) Upon entering the body, CH3H9+ reacts with cysteine to form a molecule that is able to pass through the blood brain barrier (BBB). Draw the structure of this molecule and purpose why it is able to pass through the BBB (Hint: think about another amino acid). B) The adduct formed in part A is very labile. On encountering selenocysteine, it can permanently inhibit it. Propose how the adduct from Part A inhibits selenocysteine and explain your answer.arrow_forwardYou have an unknown heptapeptide that gives the following amino acids after acid hydrolysis (2M.2K,R, A,P) treatment with CNBr gives hormoserine lactone (M*), a tetrapeptide (2K,M*,A) and (P,R). Treatment with trypsin gives free P, free K, (A,K,M) and (R,M). what is the sequence of amino acids for the heptapeptide? show work.arrow_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