Biochemistry 3304 Review LeggeCorrect Answers Shown in RedI. True or False?T F 1. Myoglobin is characterized by a Hill coefficient that is a negative number.T F 2.Single amino acid mutations in proteins in humans are always detrimental eventually resulting in disease.T F 3. DEAE-cellulose resin binds proteins that possess a net negative charge.T F 4. Peptide bonds are usually trans.T F 5.Enzymes can alter the reaction conditions to allow non-spontaneous reactions to occur.T F 6.NAD+ can be an important reductant in redox reactions. T F7.A catalyst acts by lowering yhe activation barrier for the reaction being catalyzed.T F 8 One turnover by succinate dehydrogenase yields one equivalent of FADH2.T F9Michaelis-Mentin kinetics assumes that the Michaelis complex is consistently increasing over the course of the enzyme reaction.T F 10. Trypsin specificity is conferred by a deep hydrophobic (non-polar) pocket.II. CalculationsThe molecular weight of SDS is 223 g/mole. Calculate how much SDS you would need to make 100 ml of the following solutions:11. 200 mM SDSA. 4.5 B. 0.0045 g SDSC. 4.5 kg SDSD. 4.5 mg SDSE. 4.5 g SDS12. 20 % SDSA. 446 g SDS B. 446 mg SDSC. 20 g SDSD. 20 mg SDSE. 2.0 g SDS13. 20 mg/ml SDSA. 2.0 g SDS B. 2.0 mg SDSC. 4.5 mg SDSD. 0.45 mg SDSE. 4.5 g SDSBiochemistry 3304 Review LeggeBiochemistry 3304 Review LeggeIII. MatchingBelow are five graphs in which the solid line indicates oxygen binding to a pure homogenous hemoglobin solution. Choose which graph (“A – E”) best represents the following scenarios? Note: “A – E” may be used more than once.C _____ ___ 14. The dashed line representing an increase in the pH of the hemoglobin solution.B ______ __ 15. The dashed line representing the oxygen binding curve of myoglobin. 1.00.750.50.25Increasing pO2 (torr)AYO2 1.00.750.50.25Increasing pO2 (torr)BYO2 1.00.750.50.25Increasing pO2 (torr)CYO2 1.00.750.50.25Increasing pO2 (torr)DYO2 1.00.750.50.25Increasing pO2 (torr)EYO2Biochemistry 3304 Review LeggeIV. Other multiple-choice questions (# 16 – 20). Choose the most correct answer.During your Senior Honor’s thesis work, you isolated five new proteins and determined theirmolecular weights and pI’s. Your thesis advisor gave you the opportunity to name them since youdiscovered them. You think hard about what you want to name them and decide you will namethem after your favorite mentors and teachers. You prepare a table in alphabetical order of eachprotein’s name to organize your new proteins and their characteristics as follow:Protein Name Molecular Weight (kDa) pIProtein “Briggs” 100 5.0Protein “Fox” 250 10.0Protein “Legge” 80 6.8Protein “Tu” 15 4.5Protein “Yeo” 45 9.516. Your thesis advisor asks you to go back and do another purification to isolate more of yourproteins for characterization. You decide to try and change the conditions to optimizepurification. The first column that you decide to try is a DEAE-cellulose column which isequilibrated in a buffer at pH 7.0. Which of the proteins listed below will NOT bind to thecolumn? A. FoxB. LeggeC. TuD. Both “A.” and “B.”E. All of the above17. In order to elute the bound proteins from the DEAE cellulose column in #11, you can use which of the following method (s)? A. Increase the salt concentration.B. Decrease the pH of the buffer on the column.C. Increase the pH of the buffer on the column.D. Either “A.” or “B.”E. Either “A.” or “C.” 18. Which of your proteins would migrate the furthest or the longest distance on an SDS-PAGE gel? A. BriggsB. FoxC. LeggeD. TuE. Yeo19. In a gel filtration experiment, the order that your proteins would elute would most likely be as follows:A. Briggs, Fox, Legge, Tu, YeoB. Fox, Briggs, Legge, Tu, YeoC. Tu, Yeo, Legge, Briggs, FoxD. Fox, Briggs, Legge, Yeo, TuBiochemistry 3304 Review LeggeE. Briggs, Fox, Yeo, Tu, LeggeBiochemistry 3304 Review Legge20. Which of the following molecule is considered a denaturant?A. UreaB. Ampholytes C. LysozymeD. Ammonium sulfateE. NADH21. A reaction with H = 11 kJ/mol and S =40 J/K·mol, at 27C, is:A. spontaneousB. non-spontaneousC. at equilibriumD. impossible to determine reactivityE. none of the above22. What is the [OH–] in a 0.05 M HCl solution? A. 5 × 10–12 MB. 1 × 10–13 MC. 2 × 10–13 M D. 5 × 10–13 ME. 2 × 10–14 M23. Which of the following amino acids has a sulfur atom in its side chain?A. AsnB. SerC. CysD. PheE. None of the above24. How many possible sequences are there for a tetrapeptide using the 20 amino acids? A. 80B. 256C. 2,560D. 25,600E. 160,00025. Trypsin digestion of a peptide yields the fragments (H, MNK, IMR, and LMR). Cyanogen bromide treatment yields (RH, RM, NKIM, and LM). What is the sequence of the intact peptide?A. NKIMRHLMRMB. LMRHNKIMRMC. LMRMNKIMRHD. LMRIMRMNKHBiochemistry 3304 Review LeggeE. NKIMLMRHRMBiochemistry 3304 Review LeggeShown below is a titration curve for glutamic acid. Examine the structures of the glutamic acid species (A – E) below. Choose the correct answer from “A – E” (questions #26-28). Note: “EtOH – E” may be used more than once. 26. What is the structure of the species that predominates at the labeled point “ 1 ”? ________A27. What is the structure of the species that predominates at the labeled point “ 5 ”? ________D28. Which of the structures cannot exist as shown at any pH in aqueous solution? _________C A. B. C. D. E.29. Which one of these characteristics is not true for the α-helix?A. There are 3.6 amino acids per turn.B. There is a requirement for glycine every third amino acid residue.C. A hydrogen bond forms between the carbonyl oxygen of the nth amino acid residue and the —NH group of the (n + 4)th amino acid residue.D. Proline is typically not found in the α helix.E. It is right-handed.H1311 9 7 5 3pHEquivalents of base1 2 3123456Biochemistry 3304 Review Legge30. Which amino acid can stabilize protein structures by forming covalent cross-links between polypeptide chains?A. MetB. SerC. GluD. GlyE. Cys31. The value of n in the Hill equation for hemoglobin is about ______as great as the value for myoglobin.A. halfB. twiceC. three timesD. five timesE. ten times32. Conformtion(s) that has (have) both a