Please don't copy Consider the following two peptide sequences.Peptide 1): LKAENDEAARAMSEAPeptide 2): CRAGGFPWDQPGTSNDraw an ideal Circu lar Dichroism spectra "CD" for the secondary structure of these two peptide sequences.Explain your answer.

The amino-acids sequences have different propensities for forming secondary structures. based on the…

Answered: Consider the following two peptide…

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 sequence of a 29 aa long peptide can be determined from the following data: Treatment of the peptide with dansyl chloride reveals that the amino-terminal is Val. Trypsin digestion, separation of peptides, and Edmann technique give the sequences for peptide fragments as follows: T-1 V-G-A-H-A-G-E-Y-G-A-E-A-T-E T-2 A-A-W-G-KT-3 V-L-S-P-A-K T-4 T-N-V-K
On the paper provided, draw the chemical structure of a peptide with a sequence LEMD at pH 7. The pKa values for the amino acid sidechain of E and D are 4.1 and 3.9, respectively.
Draw the structure of peptides TGPNLHGLFGR and ELAGAPPEPA, and calculate m/z values of their an, bn, and yn sequence ions.
The sequence of a 29 aa long peptide can be determined from the following data. a) Treatment of the peptide with dansyl chloride reveals that the amino terminal is Val. b) Trypsin digestion, separation of peptides and Edman degradation give sequences for peptide fragments as follows: Val-Gly-Ala-His-Ala-Gly-Glu-Tyr-Gly-Ala-Glu-Ala-Thr-Glu Ala-Ala-Trp-Gly-Lys Val-Leu-Ser-Pro-Ala-Lys Thr-Asn-Val-Lys c) Chymotrypsin digestion, separation of peptides, and Edman degradation give the following sequences for fragments: Gly-Ala-Glu-Ala-Thr-Glu Gly-Lys-Val-Gly-Ala-His-Ala-Gly-Glu-Tyr Val-Leu-Ser-Pro-Ala-Lys-Thr-Asn-Val-Lys-Ala-Ala-Trp What is the sequence for the peptide?
a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain
Predict the secondary and tertiary structure of the following peptide sequence: a.) LKAENDEAARAMSEA b.) CRAGGFPWDQPGTSN 2.) In an experiment, you somehow added cysteine so that it would covalently bond a protein complex composed of two proteins. But, the problem is you can’t detect the bridge, meaning you can’t detect covalent bond formation of cysteine in between two proteins. How do you generate disulfide bond? Give an idea to force disulfide bond formation between two proteins. 3.)Lysozyme consist of 4 disulfide bridges while Bovine Serum Albumin(BSA) is 17. However, lysozyme is more rigid compared to BSA. Why? What are the factors affecting the rigidity of their structures? Does the number of α-helixes and β-sheets matter?
Three peptides were obtained from a trypsin digestion of two different polypeptides. indicate the possible sequences from the given data and tell what further experiment should be carried out in order to determine the primary structure of the polypeptide. Polypeptide II: 1. Val-Leu-Gly-Glu 2. Ala-Glu-Pro-Arg 3. Ala-Met-Gly-Lys
The globular proteins tend to have a high-dimensional folding in their higher-order structure g providing very limited analysis when conducting peptide analysis. Explain what steps would be suitable to prepare a successful chromatographic peptide mapping?
Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show them in zig-zag style, from amino to carboxy terminus, with correct stereochemistry Draw the predominant form at pH = 2 Draw the predominant form at pH = 5 Draw the predominant form at pH = 7 Draw the predominant form at pH = 12
A biotechnology company focused on peptide therapeutics is investigating the properties of several peptides for a variety of applications. Their sequences are given below: Pep A: NGSLGAAGRG Pep B: KKALLAHALH Pep C: LVQAIFPTPS a. What is the net charge of each sequence at pH 7 (to the nearest 0.1 charge unit)? b. Which peptide sequence would be most likely to be part of an intrinsically ordered domain in a protein? Explain. c. Which peptide would likely be best suited as part of a pH-sensitive drug carrier that is designed to change its charge between neutral pH and endosomal pH (which is between 5 and 6)? Explain. d. Which peptide sequence would be most likely to be buried in the interior of a protein? Explain.
Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. [References] If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced by another amino group, what would be the predominant form of this amino acid at pH 12 if the pK, value were 10 for the unique amino group? (Select all that apply.) Both of the carboxyl groups are deprotonated. The amino acid-carries a negative 2 charge. The amino acid carries a negative 4 charge. The amino groups are in the form -NH". Both of the amino groups are deprotonated.
Partial hydrolysis of a protein yielded a number of polypeptides. One of them was purified. Deduce the sequence of amino acids in this polypeptide from the following information: (a) Complete acid hydrolysis yielded ala + arg + 2ser + lys + phe + met + trp + pro (b) Treatment with fluorodinitrobenzene (FDNB, the Sanger reagent) followed by complete acid hydrolysis yielded dinitrophenylalanine (DNP-ala) and a dinitrophenyllysine (e-DNP-lys) as the only DNP derivatives. (c) Neither carboxypeptidase A nor carboxypeptidase B released a C-terminal amino acid. (d) Treatment with cyanogen bromide (CNBr) yielded two peptides: One contained ser + trp + pro. The other contained all the remaining amino acids (including the second ser). (e) Treatment with chymotrypsin yielded three peptides. One contained only ser + pro. Another contained only met + trp. The third contained phe + lys + ser + arg + ala. (f) Treatment with trypsin yielded three peptides. One contained only ala + arg. Another…

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Consider the following two peptide sequences. Peptide 1): LKAENDEA ARAMSEA Peptide 2): CRAGGFPWDQPGTSN Draw an ideal Circular Dichro ism spectra "CD" for the secondary structure of these two peptide sequences. Explain your answer.