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).

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.

Consider the following fatty acid attached below.    a) What is the number convention for this fatty acid above, including the location of the double bond from the α carbon end? Remember to use the Δ (delta) in your answer for the double bond location b) What is the ω (omega) numbering of the double bond for the fatty acid above? c) What is the product after two hypothetical additional rounds of synthesis for the fatty acid? Remember that synthesis adds 2 carbons at a time to the carboxylic end.

The equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]

H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14

The enzymatic activity of lysozyme is optimal at pH 5.2 and decreases above and below this pH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu35 and Asp52. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5 respectively. What is the ionization state of each residue at the pH optimum of lysozyme? How can the ionization states of these 2 amino acid residues explain the pH-activity profile of lysozyme?

Draw the linear fisher projections of D-ribarnic acid, L-xyluronic acid, D-arabinuronic acid, L-gluconate, D-mannarate, L-idarate and D-galacturonate, and D-lyxonate

Draw the enediolate intermediate of the ribulose-5-phosphate isomerasereaction (Ru5P → R5P).

Write a structural formula for a tetrapeptide composed of phenyl-alanine, glycine, aspartic acid, and histidine in which the phenylalanine is N-terminal and the histidine is C-terminal. How many different tetrapeptides could be written that fit the criteria in this question?

The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is A