asap pls Amino acid analysis of a HEPTAPEPTIDE reveals the following information below:(NOTE: when the sequence is not known, a comma separates the amino acids)R and modifiedfree amino acidsPeptide 1(K, R, V)HydrazinePeptide 2(K, M, W, Y)HEPTAPEPTIDECleavage withCyanogenbromide, thenchromatography1. What is the N-terminal residue?Cleavage with Chymotrypsin,then chromatographyCleavage with Thermolysin,then chromatography2. What is the sequence of Peptide 1?6N HCL, 100 °C, 24 hPhenylisothiocyanate3. What is the sequence of Peptide 3?4. What is the sequence of Peptide 5?When answering the questions below, please use the ONE-LETTER CODE (UPPERCASE) for the amino acid, with NO spaces and symbols between each letter.5. What is the overall amino acid sequence?K, K, M, R, V, W, YPTH derivative of YPeptide 3 (K, M, R, V)Peptide 4 (K, W)Free YPeptide 5 (K, Y)Peptide 6 (R, V)Peptide 7 (K, M, W)

The proteins are composed of sequence of amino acids connected via peptide bonds. The sequence of…

Answered: Amino acid analysis of a HEPTAPEPTIDE…

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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Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide.
Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide. I don't understand how the order of amino acids in Step 2 was arranged. Please explain. Thank you.
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
In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%
Draw an ionization scheme for each of the amino acids Phenylalanine, Methionine, Tyrosine, Asparagine (from the most acidic form to the most basic form) , and show your computation for the pI/IP of each of the amino acids as well. Draw a complete structural representation for the tetrapeptide Phe-Met-Tyr-Asn (NOTE:use the zwitterion form) Give the IUPAC name for the tetrapeptide formation of F-M-Y-N. List all the possible tetrapeptide formed from one of each amino acids Phe-Met-Tyr-Asn? (NOTE: Use the three letter abbreviation code for the amino acids in answering D)
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
Determine the Primary amino acid sequence of an Octapeptide Composition · Tyr , Arg，Pro, Lys ,Lys ,Met ,Trp，Phe N terminal 1 2 3 4 5 6 7 8 C terminal 1) Treatment with an Edman reagent gives a PTH-AA that shows a Yellow color with Ninhydrin. 2) Trypsin digestion of the Octapeptide gives tetepeptide, dipeptide， free Arg ，free Trp. 3）CNBr = pentapeptide and tripeptide. 4) chymotrysin - tetapeptide and two dipeptiele. The tetrapeptide contains an amino acid with an OH group in the side chain.
Consider the following peptide to answer the questions below: A M A K K E S H I F T A I D E What is the total charge of this peptide at pH = 5? What is the N terminal amino acid (full name)? C terminal amino acid? How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)? Would this peptide be a candidate to form an alpha helix? Why or why not
Draw the following sugars using Haworth projections:a. b-d-galactopyranose b. a-d-tagatopyranose c. a-l-glucopyranose
Why different amino acids have different Rf values? If you separate a mixture of amino acids consist of glutamic acid, histidine, glycine, tryptophan and isoleucine with paper chromatography using NH3: Benzene (10:90) as a mobile phase what do you expect the Rf values of the amino acids will be?
You have isolated the following peptide: His-Ser-Arg-Ala-Glu-Leu-Pro-Gly A) Calculate the approximate charge of this peptide at pH 1, pH 3, pH 5, pH8, pH 11, and pH 14. B) What is the PI of this peptide?
you have isolated the following peptide: His-Ser-Arg- Ala-Glu- Leu- Pro- Gly Calculate the approximate charge of the peptide at Ph 1, 3, 5, 8, 11, 14 AND what is the PI of this peptide?

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