Determine the primary structure of pentadecapeptide X, based on the following results.A). Reagent: merchapthoethanolReleased two fragments, namely:1. pentapeptide (Y), amino acid composition: cys, phe, ser, thr, val2. decapeptide (Z), amino acid composition: ala(2), cys, leu, lys, phe, pro, tyr,B). Process: Edman Degradation1. Nt of peptide Y is ser, 2. Nt of peptide Z is ala.C). Enzyme: Carboxypeptidase A1. val was released from peptide Y; 2. no amino acid was released from peptide ZD). Enzyme: Chymotrypsin1. peptide Y released two fragments with the following amino acid composition.(phe, ser, thr)(cys, val)2. peptide Z released three fragments with the following amino acid composition3.val(2)(ala [2], tyr)10(cys, phe)(leu, lys, val, pro, val)E). Enzyme: trypsinpeptide Z released two fragments with the following amino acid compositionala (2), cys, leu, lys, phe, tyrval (2), pro

Determination of protein primary structure is done by degradation with different enzymes which have…

Answered: 3. Determine the primary structure of…

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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Bb.45.
VII. Analysis of a peptide antibiotic purified from a strain of Bacillus brevii resulted in the following significant information: Complete hydrolysis of the peptide yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val Molecular weight of the peptide was estimated to be aroung 1,200 Da The peptide failed to undergo hydrolysis when treated with carboxypeptidase Partial hydrolysis and then chromatographic separation of products yielded the following di- and tripeptides: Leu-Phe, Phe-Pro, Orn-Leu, Val-Orn, Val-Orn-Leu, Phe-Pro-Val, Pro-Val-Orn Treament with dinitrofluorobenzene (DNFB) followed by complete hydrolysis yielded only free amino acids and the DNFB-derivatized ornithine at its side chain Using this set of information available to you, deduce the amino acid sequence of this peptide antibiotic. Write your final peptide sequence only using 3-letter abbreviations.
1. Amino acid analysis of the peptide gave the following residues: Asp Leu Lys Met Phe Tyr. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was C-C-CH2. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys. What is the amino acid sequence for this heptapeptide?
The cofactor shown below: is an oxidizing agent is a reducing agent is a carrier of acyl groups is flavin mononucleotide The cofactor shown below: CH2 HC OH HC OH HC OH CH2 H₂C NH H H H OH OH NH₂ 1) is an oxidizing agent 2) is a reducing agent 3) is a carrier of acyl groups 4) is flavin mononucleotide
1. Analysis of a peptide antibiotic purified from a strain of Bacillus brevii resulted in the following significant information: - Complete hydrolysis of the peptide yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val - Molecular weight of the peptide was estimated to be aroung 1,200 Da - The peptide failed to undergo hydrolysis when treated with carboxypeptidase - Partial hydrolysis and then chromatographic separation of products yielded the following di- and tripeptides: Leu-Phe, Phe-Pro, Orn-Leu, Val-Orn, Val-Orn-Leu, Phe-Pro-Val, Pro-Val- - Orn Treament with dinitrofluorobenzene (DNFB) followed by complete hydrolysis yielded only free amino acids and the DNFB-derivatized ornithine at its side chain By using the above information, deduce the amino acid sequence of this peptide antibiotic. Write the final peptide sequence using 3-letter abbreviations. Show the complete and step by step solution.
25) Below are two amino acids: cysteine and histidine. a) Draw the reaction mechanism of a dehydration synthesis reaction between cysteine and histidine below: HS H Product 1 N OH HN H b) Draw two different products of the dehydration synthesis reaction from part a). Prove that these are two different products by labelling the N and C termini, peptide bond, and R-groups of each product. Product 2 OH
1. Label the ALPHA-Carbon, AMINO Group, CARBOXYL Group, and AMINO Side Chain of the following amino acids:- Proline- Glycine- Aspartic acid- Asparagine- Lysine 2. Write the structure of the following polypeptide chainsa.) Asp-Leu-Serb.) Thr-Trpc.) Gln-Ala-Prod.) Ile-Met-Cys-Glu
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal -NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu–His-Phe-Arg–Trp–Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu–Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu-His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala | (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu–Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala (a) Which of the three peptides would elute first from a gel filtration column? (b) Which of the three peptides would migrate the fastest on SDS-PAGE (c) Which of the three peptides could be…
7. Consider the structures shown. For each structure select all that apply. a) pentose, hexose or heptose b) D or L c) ketose or aldose d) a or ẞ e) pyranose or furanose COOM CHACH Structure A Structure C
A) what does the figure illustrate? B) Label the components in the figure pointed by the arrows and briefly mention the bonding partners involved in each case
2) Consider the following disaccharide which was formed from the breakdown of a polysaccharide found in plant material. ОН Glycosidic linkage: H H OH H H НО H H. OH H. ОН OH H НО H ОН a. Label the glycosidic linkage above in the following format: a/B(# → #) b. Would you expect this disaccharide to have been formed from amylose or amylopectin? c. Describe at least two chemical tests that would give insight into the structure of this disaccharide, assuming you've isolated it and wanted to elucidate the structure from scratch. Include detail on not only the tests you would use but what results you would expect to get given the structure above. Assume you can analyze the structure of any monosaccharide you get from your chemical tests.

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