Draw the structure of the protected amino acid that must be anchored to the solid support in order to use a Merrifield synthesis to prepare leucine enkephalin. Include stereochemistry in your answer. Do NOT explicitly draw any hydrogen atoms in your structure or use abbreviations like OME, COOH or Ph. (N terminus) Try-Gly-Gly-Phe-Leu (C terminus)
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- Agamemnon just got his first octapeptide to sequence. Identify the correct sequence from the data gathered below. He first did a complete acid hydrolysis and identified the amino acids using HPLC. He found he had a lle, Ala, Ser, Asp, Asn, Phe, His, and an Arg. He submitted the octapeptide to conditions of Edman degradation and got the structure below. H. но He used carboxypeptidase and generated a His and a heptapeptide. He used chymotrypsin and generated a5-amino acid sequence and a 3-amino acid sequence. He used trypsin and generated a 2-amino acid sequence and a 6-amino acid sequence. Partial hydrolysis of the nonapeptide yielded the fragments RIS, NAH, and SF among others.Modify isoleucine to show its structure at pH 1 and pH 13. Modify each amino acid by adding or removing atoms or bonds and by adding charges where appropriate. pH 1 pH 13 Select Draw Rings More Erase Rings More Erase C с CH₂ CH₂ H₂C H₂N 1 CH₂ | CH | 310 H― H O H N U с || 0 H Q2 Q Select Draw / ||| ||| H₂C H₂N 1 CH₂ | CH - n O H | H 0 H N H Q2QHoping for solutions since I’m having a hard time with this. Pls skip if unsure or not willing to answer the subitems (these are all connected for one item). Thanks in advanced. Kriel just discovered a new protein, Krielase and for it not to unfold and lose its function, he realized that the protein needs to be constantly immersed in a pH = 6.50 solution. He is therefore interested in preparing a 50 mL 0.08 M pH = 4.50 buffer to contain the protein. He listed down the pure acids available to his disposal, and also looked for their acid dissociation constant (Ka) values. Acid Name Ka1 Ka2 Ka3 Nitrous Acid (HNO2) 4.00 x 10-4 N/A N/A Acetic Acid (CH3COOH) 1.76 x 10-5 N/A N/A Ascorbic Acid (HAsc) 7.90 x 10-5 1.60 x 10-12 N/A Phosphoric Acid (H3PO4) 7.52 x 10-3 6.23 x 10-8 4.28 x 10-13 A. Identify which weak acid system is best to use in preparing the buffer? Why? B. Identify the species which will make up the buffer system?…
- 1 Submit Q10. !! Unanswered Q10. An average amino acid is about 110 Da (Daltons). If there are 1273 amino acids in the SARS-CoV-2 spike protein, what do you expect the mass of spike to be? How does that compare to the expected mass of about 200 KDa? more than expected by about 90 Da Less than expected by about 90 Da B. more than expected by by about 60 KDa less than expected by about 60 KDa Submit odf 0/11 answeredIn the dreaded Zephyer galaxy there is a race of Fairies that have the ability to change their body pH very dramatically. A group dragons are study how amino acids behave in the fairies populations. Please draw and upload the the following peptide at pH= 7, Determine the charge on the amino acid chain at pH=1,pH-11, pH- 7. And explain if their is any disulfide bonds. LADENAngiotensin II is a polypeptide that regulates blood pressure. 2nd attempt Enter the amino acids, in order, as three-letter abbreviations, separated by hyphens. Start at the N-terminal end. Which amino acids are in the structure? HN HN. NH₂ NH₂ НО. NH NH NH asp-arg-val-tyr-lle-his-pro-phet HO- NH HO- **** HN Angiotensin II NH NH See Periodic Table Se
- Your task is to categorize and tabulate the 20 standard amino acids with the following columns: 1. Amino Acid Full Name (alphabetical order) 2. One letter abbreviation 3. Three-letter abbreviation 4. Structure of R-group (if you will present the full picture of the amino acid, encircle or highlight the R group) 5. Classification (1, 2, 3 or 4) 6. Essential or Non-Essential Amino Acid (research on this; write E for Essential & NE for Non-Essential) 7. Use/ Function of Amino Acid5. Draw a schematic illustrating the overall iteration process for solid phase peptide synthesis. You do not need to use specific chemical structures, but your overall depiction should be clear.Region/point where AA is predominantly present as a (-1) charged species? The effective buffering range for the amino acid in the acidic region? Region/point where the solution has 50:50 percent mixture of the (0) and (-1) species
- How many of the -amino acids shown in Table 26-1 contain aromatic rings? How many contain sulfur? How many contain alcohols? How many contain hydrocarbon side chains?You may use the following table of pKa values for typical amino acid substituents. alpha carboxylate group Sidechain carboxylate Imidazole alpha amino group Guanidino group First [Select] 2 [Select] 4 Thiol sidechain amino group Consider the following 3 peptides. Last 6 9 12 8 Peptide 1: E-H-A-D-E-K Peptide 2: E-D-R-H-Y-G Peptide 3: G-E-G-D-S-D What would be the order of elution of these peptides for a anion exchange column at pH 7.0? 11 [Select]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] >