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- 1a. suggest a test you will use to show that a given food substance contains protein. b. show how you will use i. modified Gabriels synthesis ii. Streckers synthesis to prepare phenylalanine in the laboratory. 2a. Describe in details how you will determine the primary structure of protein. b. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows, Histidine 7.64 Lysine 9.74 Cysteine 5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components. 3a. A decapeptide has the following amino acid composition, Ala2, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides, Cys-Glu-Leu +Gly-Arg-Ala +Lys-Val-Phe-Gly Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylsine. From the experimental data, deduce the primary structure of the…Brucine is a poisonous alkaloid obtained from Strychnos nux vomica, a tree that grows in India, Sri Lanka, and northern Australia. Write out a resolution scheme, which shows how a racemic mixture of phenylalanine can be resolved using brucine.Triethylenemelamine (TEM) is an antitumor agent. Its activity is due to its ability to cross-link DNA. a. Explain why it can be used only under slightly acidic conditions. b. Explain why it can cross-link DNA.
- Triethylenemelamine (TEM) is an antitumor agent. Its activity is due to its ability to cross-link DNA. a. Explain why it can be used only under slightly acidic conditions.b. Explain why it can cross-link DNA.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.Interpret the mechanism of clorazepate
- please explain why this happends, im having trouble in this section. Part A Chymotrypsin, an enzyme that hydrolyzes peptide bonds in proteins, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of the chymotrypsin-catalyzed reaction affected by each of the following conditions?An 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.A reactive nucleotide building block obtained by the reaction (9) which occurs in the presence of a weak base diisoprpylethlamine. Write down a detailed mechanism for the reaction 9
- Bradykinin is a linear nonapeptide released by blood plasma globulin in response to a wasp sting. It is a very potent pain-causing agent. Its constituent amino acids are 2R, G, 2F, 3P, S. The sue of 2,4-dinitrofluorobenzene and carboxypeptidase shows that both terminal residues are arginine. Partial hydrolysis of bradykinin gives the following di- and tripeptides: FS + PGF +PP + SPF + FR + RPMatch the following methods of Analysis Fractional analysis, methylation, and periodate oxidation Use of endo- and exoglycosidases Polarimetry, mass spectrometry, & NMR Chromatographic separations of hydrolyzed fragments A. Chemical Method B. Enzymatic Method C. No Match D. Spectroscopiclactic acid was disscolved in an aqueous solution at a ph of 4.9 the pka of lactic acid dissociation is 3.9 what are the fractions of positiviely negatively and neutrally charged molecules of lactic acid in the solution