Don't use extra explanation solve correct Handwritten.PART A.Write the structure of the following peptides in a bond paper and upload as pdf file.Expanded structure.Use red ink for peptide bond. [For your reference download all the amino acids with the three and single letter symbol](possible points 9)a) threonyl leucyl asparagyl alanineb) glycyl tyrosyl histidyl glutamic acidc) phenylalanyl valyl arginyl seryl tryptophan

Answered: Image /qna-images/answer/072c0df6-35af-4378-b70b-669f90dfc5f1.jpg

Answered: Handwritten. PART A. Write the…

Organic And Biological Chemistry

7th Edition

ISBN:9781305081079

Author:STOKER, H. Stephen (howard Stephen)

Publisher:STOKER, H. Stephen (howard Stephen)

Chapter9: Proteins

Section: Chapter Questions

Problem 9.58EP

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Similar questions

a) A solution of amino acid having carboxylic side chain was titrated against NaOH. If initial pH of the solution was 2.8. Describe the state of the functional groups of the amino acid at the initial pH and at 10.5.b) Briefly explain how you will separate amino acids mixture using the charge difference between the amino acids. c) A given glycine solution was titrated against NaOH and pH of the final solution was 4.8. Given that pKa1 and pKa2 of glycine are 2.34 and 9.60, respectively. Calculate the concentration of the dissociated amino acid in terms of the undissociated amino acid, if [x] and [y] are the concentrations of dissociated and undissociated amino acid, respectively.
Considering the peptide structure on the image, label N-terminus and C-terminus, circle each of the peptide (amide) bonds, and provide the primary sequence of the protein using three letter abreviaciones for the amino acids
One of the most advanced methods for determining a protein sequence is tandem mass spectrometry (MS/MS). Select from the list of statements below all that applies to MS/MS. Group of answer choices CID is one way of performing tandem MS experiments The experiment start by chopping the protein into smaller peptide fragments using an enzyme These peptide fragments are later introduced into the mass spectrometer to determine their molecular weight Peptide fragments are selected for further fragmentation by collision with an inert gas There are only 4 types of ions which can result from MS/MS fragmentation: a, b, x, and y ions The a and b ions are the ones with the original C terminus, whereas the x and y ions are the ones with the original N-terminus All of the above
What is the amino terminal residue? What is the carboxyl terminal residue? How many amino acid residues are in the peptide? The net charge of this peptide at pH 7.4 would be?
The denaturing of proteins occurs when the stabilizing forces are altered. Below is the set of processes in which proteins are denatured. Classify the following processes according to the denaturing agent involved. Please help me understand the diff and correct any mistakes.
A peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly The p?a values for the peptide’s side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side‑chain pKa glutamate 9.609.60 2.342.34 4.254.25 histidine 9.179.17 1.821.82 6.006.00 tryptophan 9.399.39 2.382.38 serine 9.159.15 2.212.21 glycine 9.609.60 2.342.34 leucine 9.609.60 2.362.36 arginine 9.049.04 2.172.17 12.4812.48 proline 10.9610.96 1.991.99 Calculate the net charge of the molecule at pH 11 and estimate the isoelectric point (pI)(pI) for this peptide.
Please help me with the following 1) sketch a phosphodiester bond 2) Make the two amino from the image below. And contrast the polarity of the side chains
Give the sequence of the following tetrapeptide:
A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)
Using both three- and one-letter codes for amino acids, write the structures of all possible peptides containing the following amino acids: (a) Val, Ser, Leu (b) Ser, Leu2, Pro
On complete hydrolysis, a polypeptide gives two alanine, one leucine, one methionine, one phenylalanine, and one valine residue. Partial hydrolysis gives the following fragments: Ala-Phe, Leu-Met, Val-Ala, Phe-Leu. It is known that the first amino acid in the sequence is valine and the last one is methionine. What is the complete sequence of amino acids?
The -helical parts of myoglobin and other proteins stop whenever a proline residue is encountered in the chain. Why is proline never present in a protein helix?

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