can someone draw this out please 4)a) Draw the tripeptide Tyr-Pro-Lys once with a trans peptide bond between Tyrand Pro and once with a cis peptide bond between Tyr and Pro.b) The electrospray ionization mass spectrum (ESI-MS) of the tripeptide youdesigned in part (a) shows peaks indicative of mono-protonation and di-protonation of the tripeptide. At what values of m/z would these peaks beexpected (no fragmentation)? Briefly explain your answer (showing yourworkings).

Detailed explanation:a) Drawing the Tripeptide Tyr-Pro-LysTrans Peptide Bond between Tyr and Pro: In…

Answered: 4) a) Draw the tripeptide Tyr-Pro-Lys…

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter26: Biomolecules: Amino Acids, Peptides, And Proteins

Section26.SE: Something Extra

Problem 20VC

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(a)Draw Histidine in all its protonated form and include the pKa's where appropriate. (b) Calculate the fraction of histidine that has its imidazole side chain protonated at pH7.3. The pKa values for histidine are pK1 = 1.8, pKr (imidazole) = 6.0, and pK2 = 9.2
2) Part of the 'H NMR spectrum for a dipeptide recorded in D₂O is shown below. The signal for the CH 3 group is not shown. (i) Explain what has happened to the H-atoms attached to the N atoms. (ii) Interpret the spectrum Note the signals for HA and HA are subject to a second order effect. 'N- HAHA' 40 Hz H 0.1 ppm L-Ala-Gly
Bilayer leaflet CO COON 1. Unfolded peptide aqueous phase 2. Unfolded peptide in membrane 3. α-helix in membrane Figure 1: Membrane binding peptide of a glycosyltransferase is shown interacting with a membrane. Positive charges are shown as blue +, negative charges are shown as red -. 7. (3%) While the membrane binding peptide is in solution it is shown as being "un- folded" in Figure 1. (a) What is the name we give to this type of secondary structure? (Answer with 1 sentence) (b) What is a general role of this type of secondary structure in a protein? Answer with proy
On the paper provided, draw the chemical structure of a peptide with a sequence YIQV at pH 14. The pKa value of the Y sidechain is 10.1.
About a decade ago, it was more common to use peptide mass mapping to identify a protein cut from a gel. Peptide mass mapping involves digesting the protein with trypsin and then measuring the peptide masses using MALDI-TOF mass spectrometry. The more superior method of identifying a protein from a gel is to digest the protein with trypsin and then use liquid chromatography to separate the peptides. The separated peptides are then electrosprayed into a tandem mass spectrometer. The MS-MS data is uploaded into a database such as MASCOT for protein identification. Explain why the LC-MS-MS method is superior to the peptide mass mapping method.
Ph (c) For the peptide coupling reaction shown below, answer the following questions: H₂N. BOP = OH + HSO4 H₂N -N Me₂N-P Me₂N NMe2 O PF6 CH3 BOP, Hünig's base Hünig's base = ایک Dipeptide (i) Give reagents and a curved arrow mechanism for the preparation of alanine tert-butyl ester hydrogen sulfate from alanine. (ii) Provide reagents and a curved arrow mechanism for the formation of Cbz protected glutamine from glutamine hydrogen chloride. (iii) Provide a curved arrow mechanism for the peptide coupling detailed in part (c).
Shown below is a section of beta-sheet from the protein thioredoxin. Amide nitrogens are indicated by circled Ns, carbonyl oxygens by Os, and hydrogen bonds by gray lines. M strand 1 MO strand 3 (N) O 1 2 3 4 For each strand of the sheet (1, 2, 3, 4) indicate the direction (top or bottom) of the N-terminus. [Select] strand 2 [Select] O [Select] strand 4 [Select] strands 1 and 2 Determine the orientation (parallel or antiparallel) of each adjacent strand to one another. [ Select] AHO strands 2 and 3 [Select] N strands 3 and 4 [Select] >
Extintion coeficient for Y is 1280
None
T11.1. A student was provided with the following compounds: (i) N-acetyl-L-Aspartic acid (ii) tert-butyl amine and (iii) coupling agent N,N'-dicyclohexylcarbodiimide (DCC) – to create peptide(s). The synthesis was successfully completed at 100% conversion, where a 2:1 ratio of the amine to amino acid was used and all possible peptide bonds were formed. If partial racemization also took place during the synthesis, how many types of product(s) can the student possibly obtain from the reaction? HO. CH, OH Ö HN. CH, H,C NH2 (A) 1 (B) 2 (C) 3 (D) 4 (E) 5 (F) 6 (G) None of these T11.2. Referring to T11.1: assuming the synthesis was successfully completed at 100% conversion ONLY to form Dipeptide(s) while partial racemization also took place, how many types of Dipeptide product(s) can the student possibly obtain from the reaction? (A) 1 (B) 2 (C) 3 (D) 4 (E) 5 (F) 6 (G) None of these
Please consider the structural formula of the amino acid shown below when answering the following questions. Assume that the pKa values are as shown below. (A) draw the form of this amino acid that predominates at pH 8 (B) classify the amino acid as hydrophilic or hydrophobic (C) what is the net charge of this amino acid at pH 1?
Calculate the pl of arginine. Give your answer to two decimal places. pI =

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