Fig. 1 180 120 60 0 Psi -60 -120- -180- Fig. 2 180 120 60 0 Psi -180 -60 -120- -180- -120 -60 -180 -120 -60 0 Phi 0 Phi 60 60 120 180 120 180
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- Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln 8. How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. 9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. 12. Cyanogen bromide is a chemical reagent which also cleaves peptide bonds.…The bacterially produced antibiotic gramicidin A forms channels in cell membranes that allow the free diff usion of Na+ and K+ ions, thereby killing the cell. This peptide consists of a sequence of Dand L-amino acids. The sequence of a segment of fi ve amino acids in gramicidin A is R-Gly-L-Ala-D-Leu-L-Ala-D-Val-R′. Complete the Fischer projection below by adding the correct group to each vertical bond.For paper chromatography, the obtained Rf value of an amino acid with uncharged nonpolar R group is greater than the obtained Rf value of an amino acid with charged polar R goup. TRUE OR FALSE?
- The octapeptide gly-cys-met-asn-lys-ala-tyr-gly was hydrolyzed consecutively by CNBr and then trypsin (3 fragments total). The mixture of fragments was buffered at a pH 8.5 and then chromatographed on an anion-exchanger (positive resin) with the same buffer. Draw sequence (abbreviated form) of all fragments at that pH (show charges) and predict elution order.A mixture of Asparagine (pl 5.41), Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2: v First 1. Asparagine v Second 2. Aspartic Acid 3. Histidine v Third 4. Lysine v Fourth 5. Threonine v Fifth 6. No separationA mixture of Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74), Phenylalanine (pl 5.48) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2. v First 1. Aspartic Acid v Second 2. Histidine v Third 3. Lysine 4. Phenylalanine v Fourth 5. Threonine v Fifth 6. No separation
- You have isolated from a rare fungus an octapeptide that prevents baldness and you wish to determine its amino acid sequence. The amino acid composition is K2, D, Y, F, G, S, A. Reaction of the intact peptide with dansyl chloride yields dansyl-A. Cleavage with trypsin yields peptides whose compositions are: (K, A, S) and (G, F, K) plus a dipeptide. Reaction with chymotrypsin releases free D, a tetrapeptide with composition (k, S, F, A) and a tripeptide whose composition following acid hydrolysis is (G, K, Y). The enzymatic digests are each carried out on the whole, undansylated peptide.What is the sequence?The enzyme creatine kinase catalyzes the ATP-dependent phosphorylation of creatine. Propose a mechanism for the reaction described using the curved arrow convention. Show the complete structure of the nucleotide.Draw the titration curves for the following AA’s: Aspartic acid, Alanine, Lysine, Valine, Serine, and Trrosine.
- A peptide with endorphin-like property was produced and obtained from the blood. This was sequence using the protocol: Treatment with streptococcal protease gave a tripeptide and a tetrapeptide. Treatment with trypsin gave two tripeptides and an amino acid. Treatment of the 2 tripeptide products in 1.2 with 2,4-dinitrophenol gave DNP- S, and DNP-E and a mixture of amino acids. The composition of the peptide is G, E, S, and K in a 2:1:1:3 molar ratio. a. Determine the sequence of the peptide? b. Determine the pl and position in an electrophoretic profilePolyglycine, a simple polypeptide, can form a helix with ϕ = -80°,Ψ= +150°. From the Ramachandran plot, describe thishelix with respect to handedness.Name the following biomolecules. In the case of peptides, alos provide 3 - letter codes.