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- Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.the following peptide is incubated as chymotrypsin: Gly-Val-Phe-Lys-Ala. Present the detailed chemical mechanism by which chymotrypsin hydrolyzes this peptide. Briefly explain each step. Include only the structure of the final products of the reaction.The use of co-factors in catalysis: Cofactors Cofactor Origin: Structure: Catalytic role: Nicotinamide nucleotides Flavin nucleotides Adenosine phosphates Coenzyme A Biotin Coenzyme B12 Summaries the characteristics of co-factors using this table. Use both the textbook and other online sources such as Wikipedia to find the information. Under origin, report the precursor molecule e.g. “niacin” and also try to find the Vitamin X name for each compound, e.g. “Vitamin B3”. Under structure, identify the unique structural properties that allow each cofactor to perform the function it does Under catalytic role, indicate for which reactions are each of the cofactors important
- Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein. please do not copy from other answers hereThe use of co-factors in catalysis : 3.1 Metal-activated enzymes and metalloenzymes definition for each term 3.2 Cofactors Cofactor Origin Structure Catalytic role Nicotinamide nucleotides Flavin nucleotides Adenosine phosphates Coenzyme A Biotin Coenzyme B12 Summaries the characteristics of co-factors using this table. Use both the textbook and other online sources such as Wikipedia to find the information. Under origin, report the precursor molecule e.g. “niacin” and also try to find the Vitamin X name for each compound, e.g. “Vitamin B3”. Under structure, identify the unique structural properties that allow each cofactor to perform the function it does Under catalytic role, indicate for which reactions are each of the cofactors importantRadioactive uracil can be used to label all of the pyrimidine residues inDNA. Using either names or structures, present pathways for the conversionof uracil to dTTP and to dCTP. For each reaction, show the involvement ofcofactors, and identify sites of allosteric regulation. Similarly, hypoxanthine (HX) can be used to label purine residues. As given above, write reactions showing the conversion of hypoxanthine to dATP and dGTP.
- An inhibitor that specifically labels chymotrypsin at histidine 57 is N-tosylamido-l-phenylethyl chloromethylketone. How would you modify the structure of this inhibitor tolabel the active site of trypsin?Chitinase is a protein that breaks down chitin, a primary component of the cell wall in fungi, scales in fish and exoskeletons of arthropods. The activity of chitinase extracted from a plant was shown to be optimum at pH 5. You were tasked to prepare 300 mL of 150 mM buffer solution for further analysis of the extracted chitinase. REAGENTS Ka 2.5M Acetic acid Solid NaOAc•3H2O [136.08g/mol] 1.76 x 10-5 2.5M NH3 Solid NH4Cl [53.49g/mol] 5.6 x 10-10 2.5M Lactic acid Solid sodium lactate [112.06g/mol] 4.0 x 10-5 5 M HCl 5M NaOH Pls show sol'ns 1. Given the following reagents, give the moles of each component (acid & base).2. What are the mass/volume of the components needed to prepare the buffer? 3. What will the pH of the buffer be if 1mL of 5 M NaOH was added?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.
- With the aid of the simple generic diagram, identify and explain how the type of chemical bonding stabilizes a secondary structure present in 3GRS (glutathione reductase).Some of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein.