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- Rotation about the peptide bond in glycylglycine ishindered. Draw the resonance forms of the peptide bondand explain why.Amino acid isomerism (name types). Isomerism of the carbon skeleton of amino acids - give a few examples.Consider histidine as a free amino acid in aqueous solution. a) Draw the most likely structure of histidine under biochemical standard state conditions. Given that free histidine has the following three pKa values, assign each to its corresponding acidic hydrogen or conjugate base in the structure. pKa1 = 1.7; pKa2 = 6.2; and pKa3 = 9.1 b) For each pKa, give the corresponding expression for the equilibrium constant. It helps to write out the chemical equation for each. c) Create a speciation diagram for histidine by plotting Xi vs pH from pH = 4 to pH = 8 where Xi is the mole fraction of the two histidine species involved in the equilibrium constant in part b).
- Ala-Arg-Val-His-Asp-Gln Given the polypeptide chain above Estimate the net charge of the polypeptide chain at physiological pH (7.4) and at pH 5.0 . How many peptide bonds are there? What kind of polypeptide is it?Topic: ISOLATION AND CHARACTERIZATION OF PROTEINS 1. Which amino acids contains the following:a. Sulfur/sulfhydryl groupb. Aromatic groupc. Imidazole ringd. Guanidine groupe. Indole ring2. Classify the following proteins to their biological functions (casein, albumin, gluten, andmyoglobin) 3. Which level of protein structure organization are lost hydrolysis and denaturation?4. What is the Beer-Lambert’s Law? Why is it relevant to the quantitative analysis of proteins?Provide for each amino acid the names that will uniquely identify all ionisable groups at pH 11.0 and indicate individual charges associated with these groups and the overall charge of the amino acid. a. Lysine, Leucine, Histidine and Aspartate
- Draw a peptide that includes Phenylalanine, Cysteine, Tyrosine and Tryptophan. Label them by name and abbreviation. Assume a pH of 7 when drawing the protonation state of ionizable chemical groups. Why do the aforementioned aminoacids absorb U-V light?A peptide has the sequence: Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly1. What would be the net charge of the molecule at pH a) 3, b) 8, and c) 11? (Use pKa values. Do not calculate the value per se, but instead estimate considering only fully protonated, or deprotonated states. Then estimate the pI for this peptide. Show full, clear and complete procedureOptical isomerism of amino acids. L and D amino acids. Chiral centers of amino acids. Give examples of amino acids that do not have optical isomers.
- Sketch a titration curve for the following amino acids and indicate the pKa values for all titratable groups. Also indicate the pH at which this amino acid has no net charge. aspartic acid gly-valCOLOR TESTS FOR PROTEINS AND SPECIFIC AMINO ACIDS Explain why essential amino acids (EAA) are indispensable. Enumerate the EAAs. Give the structure and name of tetrapeptide, phe-asp-leu-lys.Drawing the Structure of a Glycopeptide (Integrates with Chapters 4and 5.) Consider the peptide DGNILSR, where N has a covalentlylinked galactose and S has a covalently linked glucose. Draw thestructure of this glycopeptide, and also draw titration curves for theglycopeptide and for the free peptide that would result from hydrolysis of the two sugar residues.