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.

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.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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Imagine the main chain of a protein bends back on itself, so that two amino acid residues R₁ and R₂ come close to each other. In the table below are four possibilities for what R₁ and R2 might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ R₂ specific interaction? name of specific interaction x yes alanine valine O no isoleucine asparagine ○ yes O no yes lysine glutamate ☐ O no yes threonine asparagine O no
Activation of a zymogen is by covalent modification. How might phosphorylation or dephosphorylation (also covalent modification) modify an enzyme to make it more active (or more inactive)?
Protein denaturation can alter the 3 dimensional shape of a protein alter the sequence of amino acids in protein Obreak the peptide bonds holding the protein together Other: What is the purpose of using enzyme in detergent industry? all of the statements are true Enzymes are used to remove protein stains O Enzymes are used to remove human sweat which have a tendency to adhere strongly on textile fibers O Enzymes are used to improve texture of cloth or fiber Other: When an enzyme becomes saturated with its substrate, the rate of reaction vs concentration of enzyme graph line becomes a plateau. To produce a significant change in the reaction rate O the pH must be decreased O the temperature must be increased O the concentration of the enzyme must be increased O the pH must be increased
4 How does aqueous Silver nitrate, AGNO3, works against neonatal conjunctivitis (inflammation of the outer eye) due to neonatal bacterial infection? It hydrolyzes protein in bacteria to amino acids and inactivate it. O It denatures the protein bacteria and kills them. It mutates the genetic make-up of bacteria and transforms them to useful proteins. It oxidizes side chains of cysteine residues to cystine.
Considering the peptide structure on the image, label N-terminus and C-terminus, circle each of the peptide (amide) bonds, and provide the primary sequence of the protein using three letter abreviaciones for the amino acids
A peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly The p?a values for the peptide’s side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side‑chain pKa glutamate 9.609.60 2.342.34 4.254.25 histidine 9.179.17 1.821.82 6.006.00 tryptophan 9.399.39 2.382.38 serine 9.159.15 2.212.21 glycine 9.609.60 2.342.34 leucine 9.609.60 2.362.36 arginine 9.049.04 2.172.17 12.4812.48 proline 10.9610.96 1.991.99 Calculate the net charge of the molecule at pH 11 and estimate the isoelectric point (pI)(pI) for this peptide.
Draw the structure of the following molecule The amino acid phenylalanine at pH 1
The following graph shows the activity versus pH curve for pepsin, an enzyme that breaks down proteins into smaller peptides. Estimate its optimum pH. Maximum activity No activity pH 0 pH 3.8 pH 2 O pH4 Pepsin 01 2 3 pH 4 5
10. Use the information in the table below to draw the structure of the predominant form of each amino acid at physiological pH (pH = 7.4) R side chain pKa (a-COOH) -CH₂CH(CH3)2 -(CH2)4NH2 -(CH2)2CO2H Amino acid Leucine Lysine Glutamic acid L-leucine L-lysine L-glutamic acid 2.36 2.18 2.19 pKa (α-NH3*) pKa (side chain) 9.60 8.95 9.67 10.79 4.25
4 An aqueous solution of an amino acid with a dissociable side chain is found to have the following side chain ratio at pH 4.0: K=[A- ]/[HA]=0.01. What is the identity of the amino acid?
H₂N Combination of two or more protein units 7. Which type of cross-link involves interactions between two cysteine amino acids? 8. Which type of cross-link would form between the following amino acids? Η Ο || H₂N-C-C-OH T CH₂ C=O NH₂ Η Ο LL H₂N-C-C-OH T CH₂ OH 9. To what main enzyme class do the nzym that catalyze the following reaction belong? (oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) HO | || I c-c-N-C-COO + H₂O IT HR₂ R₁ H 1 This bond is cleaved H H₂N-C-COOⓇ I R₂ Wilter navy q H I H₂N-C-C00 1 R₁ •Qisulfide 10. Briefly explain the Lock and Key enzyme model.
write structural formulas for all the ionic forms of glutamic acid, and calculate its isoelectric ph.