By using only amide/Peptide bond forming rxn and a lKylation rxns. Provide all the reaction steps with the reagent needed and conditions with out showing the mechanism for each step to form the product. Note: Use protecting groups like (Boc, Fmoc, and others) H2NNH2+
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By using only amide/Peptide bond forming rxn and a lKylation rxns. Provide all the reaction steps with the reagent needed and conditions with out showing the mechanism for each step to form the product. Note: Use protecting groups like (Boc, Fmoc, and others) H2NNH2+
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- For this reaction, a histidine amino acid residue acts as the general base while a lysine amino acid residue acts as the general acid. Draw the arrow-pushing mechanism for this reaction and make sure to include both amino acid residues mentioned above in your mechanism along with their protonation state.According to the paper, F486 is a phenylalanine residue (i.e., an amino acid that is part of a chain that forms a protein) on SARS-CoV-2. It has an important interaction with ACE2 (best seen in Fig. 1(C) and Fig. 2(A)). Looking at this phenylalanine and the green residues surrounding it, which statement best describes the interaction that could be occurring? a) It forms a hydrogen bond with Y83. b) It forms a dipole-dipole interaction with M82. c) It forms London dispersion forces with surrounding residues. d) It encounters repulsions from surrounding residues.Write out the steps needed to synthesize the following peptide using the Merrifield method.
- The reaction of ninhydrin with an -amino acid occurs in several steps (a) The first step is loss of water to give a triketone. Show the mechanism of the reaction and the structure of the triketone.(b) The second step is formation of an imine by reaction of the amino acid with the triketone. Show its structure. (c) The third step is a decarboxylation. Show the structure of the product and the mechanism of the decarboxylation reaction. (d) The fourth step is hydrolysis of an imine to yield an amine and an aldehyde. Show the structures of both products. (e) The final step is formation of the purple anion. Show the mechanism of the reactionThe stability of our genetic code depends on the stability of DNA. We are fortunate that the aminoacetal linkages ofDNA are not easily cleaved. Show why your mechanism for part (a) does not work so well with deoxycytidine anddeoxyadenosine.For an Electrophilic Aromatic substitution of Nitrobenzene and Aminobenzene predict the directing influences of the Nitro and Amino groups respectively on the incoming group. A. Nitro is strongly deactivating and meta directing ; Amino is strongly activating and ortho,para directing. B. Nitro is strongly deactivating and ortho,para directing; Amino is strongly deactivating and ortho, para directing. C. Nitro is strongly deactivating and para directing; Amino is strongly deactivating and ortho directing. D. Nitro is strongly deactivating and ortho,para directing; Amino is strongly activating and meta directing. E. Amino is strongly deactivating and ortho,para directing; Nitro is strongly activating and meta directing. F. Amino is strongly deactivating and meta directing ; Nitro is strongly activating and ortho,para directing.
- Chemistry please help with retrosynthesisAn unknown decapeptide was isolated and characterized. Complete hydrolysis of this peptide gave : F(2), A,G,C,K,N,T, W and V. Treatment with carboxypeptidase releases A. Reaction with Edman’s reagent gave PTH-T and a nonapeptide. The nonapeptide was treated with trypsin and gave 2 peptides: (V-C-G-A) and (N-FF-W-K). Give the sequence of amino acid in the decapeptide.4. Show the step-by-step process. Do not use shortcut methods. Make it as detailed as it can be. Encode (not hand-written)!
- Make an electron-flow-mechanism for this synthetic scheme. This involves predicting major and by-products using electronic and structural effects. The arrow push mechanism must be shows. (from the reaction of α-ketoacids and oxaprolines to proteins that contain native serine residues)What is the name of the peptide below and please give a synthesis for it by using solid phase peptide synthesis?Determine the primary structure of an octapeptide from the following data: Acid-catalyzed hydrolysis gives 2 Arg, Leu, Lys, Met, Phe, Ser, and Tyr. Carboxypeptidase A releases Ser. Edman’s reagent releases Leu. Treatment with cyanogen bromide forms two peptides with the following amino acid compositions: 1. Arg, Phe, Ser 2. Arg, Leu, Lys, Met, Tyr Trypsin-catalyzed hydrolysis forms the following two amino acids and two peptides: 1. Arg 2. Ser 3. Arg, Met, Phe 4. Leu, Lys, Tyr
