1. In Part II of the Procedure, you were instructed to use your original mixture of phycocyanin and 0.10M sodium phosphate buffer as your reference solution because the buffer stabilizes the protein in its native (folded) form. Briefly explain how the buffer stabilizes the phycocyanin.

Show the detailed experimental procedures for the chemical synthesis of proteins with the α-ketoacid–hydroxylamine (KAHA ligation), using (S)-5-oxaproline (Opr) as a key building block.

The pka of ascorbic acid is 4.2 at 24C. At what pH is the ratio of the deprotonated form to the protonated form 10:1? Prove using the Henderson-Hasselback equation. How to resolve this.

1. What reaction is catalyzed by the enzyme carbonic anhydrase? Which metal ion serves as a cofactor for carbonic anhydrase? Explain how this metal ion is able to assist in catalyzing the reaction.   2. In relation to enzymes, what is the difference between a cosubstrate and a prosthetic group? Give one example of each.

Lysine and tryptophan are two amino acids that contain an additional N atom in the R group bonded to the α carbon. While lysine is classified as a basic amino acid because it contains an additional basic N atom, tryptophan is classified as a neutral amino acid. Explain why this difference in classification occurs.

4. Proteases are enzymes that catalyze the hydrolysis of peptide bonds in proteins. The enzyme trypsin is a protease that specifically hydrolyzes only those peptide bonds that are formed by the carboxyl group of basic amino acid residues. Trypsin is present in the small intestine where it functions at an optimum pH of 8. Consider the pentapeptide Phe-His-Val-Lys-Glu. Draw the structures of the products formed from trypsin-catalyzed hydrolysis of this peptide.

Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though  n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds.  I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though  n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though  n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though  n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…

Amino Acids and Proteins 1. What are the structural features of amino acids with an emphasis on essential amino acids? 2. Write the properties of amino acids: zwitterion, pka, pKb, amphoteric character, isoelectric point, and electrophoresis. 3. Write the mechanism of peptide bond formation and what are its structural features. 4. What are the different types of proteins and their function? 5. Explain the meaning and importance of the primary, secondary, tertiary, and quaternary structures of a protein and the factors that cause its denaturation.

Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though  n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds.  I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though  n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though  n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though  n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…

Another method to form a peptide bond involves a two-step process:[1] Conversion of a Boc-protected amino acid to a p-nitrophenyl ester.[2] Reaction of the p-nitrophenyl ester with an amino acid ester.a. Why does a p-nitrophenyl ester “activate” the carboxy group of the first amino acid to amide formation? b. Would a p-methoxyphenyl ester perform the same function? Why or why not?