2. Draw the structure of pentapeptide Trp-Asp-Cys-Lys-Gln that would predominate in aqueous solution at pH=5.5. (Relevant pKa values are 2.2, 3.8, 8.3, 9.6 and 10.5.)
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- 1. Which peptide would be more soluble at pH 7.0, (Val)₂₀ or (Asp)₂₀ ? at pH 3.0, (Gly-Glu-Val)2. A mixture of the following amino acids (glu, leu, val, arg, ser, phe) was obtained upon complete hydrolysis of a hexapeptide. a. Edman’s reagent releases leucine b. Hexapeptide with carboxypeptidase releases serine. c. Hexapeptide with trypsin forms a tripeptide A with leucine at the N terminal and tripeptide B with valine at the N terminal. d. Tripeptide A with carboxypeptidase releases arginine and a dipeptide with glutamic acid at C terminal. e. Tripeptide B with chymotrypsin form releases serine and another dipeptide. Give: 1. the amino acid sequence of tripeptide A and B. 2. the amino acid sequence in the above hexapeptide.2. A group of peptides that influence nerve transmission in certain parts of the brain have been isolated from normal brain tissue. These peptides are known as opioids. Using the information below, determine the amino acid sequence of this particular opioid: ● Complete hydrolysis by HCl at 100° C followed by amino acid hydrolysis analysis indicated the presence of Gly, Leu, Phe, and Tyr, in a 2:1:1:1 ratio. ● Treatment of the peptide with FNDB followed by complete hydrolysis indicated the presence of 2,2-dinitrophenyl derivative of tyrosine. No free tyrosine could be found. ● Complete digestion of the peptide with chymotrypsin yielded free tyrosine and leucine, plus a tripeptide containing Phe and Gly in a 1:2 ratio. Instructions Make use of the table below to determine the sequence of the mystery protein:
- 1.One of the main sources of sphingosine in the body is in the cell membrane. What complication could arise from the biological synthesis of ceramide?4. What is the region/point where AA is predominantly present as a (-2)-charged species?5. The effective buffering range for the amino acid in the acidic region is?6. What is the region/point where the solution has a 50:50 percent mixture of the (0) and the (-1) species?6 The following structure is part of the lipopolysaccharide found on the outside of vibrio cholerae. I know that the glycosidic linkage connecting residues B and C and the glycosidic linkage connecting residues C and D are both alpha, but what are the numbers that follow the alpha? Ex: alpha- ? -> ?
- 1. Draw the structures of the 20 biologically active AA. Under each structure, write the name, one-letter code, and three-letter code followed by the AA classification based on polarity.if the tetrapeptide shown in the binding site above (Gly-Ser-His-lle) were in an aqueous solution at pH=6.2, what fraction of peptide molecules would have a +1 charge?1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensation
- 2 Please draw the arrow-pushing mechanism to create the polyketide backbone chain of TYLOSIN. If two or more extension rounds are exactly the same, you do not need to draw them more than once. However, please clearly indicate which steps are being repeated. Please draw the complete “business end” of any cofactors you use in a step1) A ligand-binding protein showing negative homotropic cooperativity? a) should give an nH value less than 1 b) should exhibit a sigmoidal binding curve c) should show a hyperbolic binding curve d) should give an nH value of 1 e) both a and b f) none of the above1. If Ser 80 was replaced with Arg what kind is the change in the bond type between these two molecules? Will this change be more or less stable. Explain