Based on the structural properties of your protein above , how resistant (or sensitive) would your protein be to heat denaturation and why
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5.
protein = D-Glucosaminate-6-phosphate Ammonia-lyase
Based on the structural properties of your protein above , how resistant (or sensitive) would your protein be to heat denaturation and why?
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- 1. Depict the structure features in the active site of cysteine protease 2. provide a step-wise reaction mechanism to show the hydrolysis of the peptide bond catalyzed by a cysteine proteasea. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
- 7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengentplease help me understand asap Please draw by hand a tripeptide of Glu, Gln, and 1 amino acid of your choice (Not Glu or Gln again) at pH 7.0 and 9.0. The only requirement is that the amino acid should be 1 of the amino acids with ionizable R groups. Peptide should have appropriate charges on groups. Please1. Draw the Fisher projection of D-glucose, and from Fisher to Haworth projection of ẞ-D-glucose. Label (R) and (S) configuration for each chiral carbon Fisher projection Haworth projection
- 3. One strategy for designing an antiviral drug against hepatitis C virus (HCV) is targeting on the viral protein NS3-4A protease, an enzyme breaking the peptide chain through a nucleophilic acyl substitution reaction on amide. The designed drug Narlaprevir with a keto amide functional group acts as a protease inhibitor undergoing a nucleophilic addition reaction. 1) Propose a reasonable mechanism for protease (viral enzyme) breaking the viral protein Enz-OH (Viral protease) R Enz НА H2N R Viral protein O:Non-enzymatic browning Proteins: Lysin, methionine Sugars: glucose, galactose, sucrose, fructose, maltose 1. Describe (the aromas produced) and the degree of browning for each solution 2. Explain variations in color with respect to each sugar-amino acid combination by taking the chemical structures of sugars and amino acids into consideration1. In the mechanism of action of triose phosphate isomerase, Lys12 is an essential amino acid in the flexible phosphate gripper loop that undergoes a large conformational change to trap the substrate in the active site excluding water and holding the phosphate group in the correct geometry for isomerization rather than dephosphorylation. What would be the effect of the mutation of Lys12 to the unusual amino acid shown below? Explain. protein backbone
- 13. Amino acid analysis of a seven residue long peptide gave Asp Leu Arg Met | Phe Met | Phe | Tyr (i) The PTH amino acid derivative released by Edman degradation was Tyr-PTH (ii) Trypsin treatment had no effect (iii) Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free Arg (iv) Brief chymotrypsin treatment yielded several products, including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Arg, and Met What is the amino acid sequence of this seven residue long peptide, and explain how you reached that conclusion?I lea the - Oligopeptide 2 a. Give the three-letter and one-letter names of the amino acids in each oligopeptide starting from the amino terminal to the carboxyl terminal. Make sure that the amino acid names are arranged in CORRECT order for both oligopeptides. I b. After complete hydrolysis, which oligopeptide will yield more ATP molecules? How many NADH and FADH2 molecules will be theoretically produced? Show all relevant computations for each oligopeptide. Tabulate your answers to keep your answers organized. ( Oligopeptide Net ATP molecules Net NADH produced Net FADH2 produced produced Oligopeptide 1 Oligopeptide 2explain the correct and wrong choices