1 Biochemistry

To the Biochem Students: Please use the following as study practice questions in preparation. I will address or go through these questions in class one week before Exam I. in the meantime I would suggest you go through each choice and try to understand why the correct answer is correct, and more importantly why the incorrect answer is indeed not the choice. These questions were designed to assist you in working through your lecture notes, powerpoint and keypoints I mentioned in class. If you feel you know the material then TEST /Evaluate yourself by doing the questions. A good study tip: try not to guess, identify if you are guessing OR really understand the concept. Again these questions and upcoming ones should be a good guide in helping you understand the lectures further. Prior to the week before the exam please see the TA if you have any questions. To help you further in finding out whether you know the information, BE CAREFUL some questions may have more than ONE answer or NO answer at all. If you are confident with your understanding you will be able to determine this correctly. BE CONFIDENT about what you do know. ON THE BLOCK Exams each question will only have ONE choice. Try to be dependent on yourself for coming up with the correct answer, if you need help feel free to see the TA on a regular basis. Try your best. I WILL DISCUSS AND GO OVER THE ANSWERS 1 WEEK BEFORE EXAM I PLEASE DO NOT PANIC, USE THESE QUESTIONS CONSTRUCTIVELY TO ASSESS HOW MUCH YOU DO KNOW

You are welcome!!

Dr. Andy Vaithilingam Chpt 1 study questions 1. Which of the following describes amino acids A. They all have the D-optical isomeric configuration B. They all have basic side chains at physiological pH C. They are stored in the human body D. Some contain an alpha amino group and an alpha carboxyl group E. They are categorized based on whether their alpha amine group is charged or not Good luck!!!

2. The following characterizes amino acids? A. Their side chains are involved in the formation of peptide bonds B. They may function as buffers C. The pKa values of the alpha amine group is usually lower than the pka value for the alpha carboxyl group D. In the formation of the peptide bond the OH group is donated by the alpha amine group E. They are only found inside cells 3. The amino acid which may be converted to pyruvate in the liver would have the following type of side chain? A. A nonpolar B. An uncharged polar C. A basic D. An acidic E. Branched

3 4. Your patient presents with muscle wasting. You would like to restore the metabolic heath status of these cells. You recall that skeletal muscle cells prefer branched amino acids as a fuel source. Thereby you would give your patient the following amino acid as a form of treatment. A. Glycine B. Serine C. Phenylalanine D. Methionine E. Isoleucine

5. Your patient presents with dizziness and problems with balance walking normally due to the accumulation of an amino in the brain which is neurotoxic. This amino acid would be categorized accordingly A. nonpolar

B. An uncharged polar C. A basic D. An acidic E. Branched 6. Which of the following amino acid may be converted to nitric oxide? A. Methionine B. Cysteine C. Tryptophan D. Arginine E. Proline

7. Which of the following amino acid may be converted to serotonin?

4 A. nonpolar B. An uncharged polar C. A basic D. An acidic E. Branched 8. The amino acid which increases the stability of tertiary protein structures through disulfide bonding may be categorized as: A. nonpolar B. An uncharged polar C. A basic D. An acidic E. Branched 9. Which of the following amino acid would be abundant in collagen? A. nonpolar B. An uncharged polar C. A basic D. An acidic E. Branched 10. Your patient has a defect in fibrillin leading to the following conclusion? A. The diagnosis would likely be MSUD B. The diagnosis would likely be sickle cell anemia C. The normal form of this protein could have proline in its primary sequence D. The diagnosis would likely be a myocardial infarction E. This defect is due to a hydrophilic globular protein 11.Which of the following types of amino acids would be abundant in histones? A. Cysteine B. Methionine

5 C. Glycine D. Lysine E. Glutamic acid 12.Free ammonia (NH3) is toxic to human tissue thereby it can be safely transported in the blood to the kidney for disposal into the tubules of the kidney for excretion. Which of the following amino acid carries out this function? A. A nonpolar B. An uncharged polar C. A basic D. An acidic E. Branched 13.Which of the following amino acid is quite frequently phosphorylated or glycosylated A. Threonine B. Glutamic acid C. Aspartic acid D. Valine E. Phenylalanine 14.Which of the following is a branched chain amino acid? A. Tyrosine B. Glutamine C. Leucine D. Asparagine E. Glycine

15.Histidine may be characterized by the following: A. It is weakly acidic

6 B. When incorporated into a protein its side chain is negatively charged C. This is an uncharged polar amino acid D. It stabilizes oxygen binding to hemoglobin E. It may be converted to nitric oxide 16.Which of the following amino acid may be converted to nitric oxide ? A. Lysine B. Arginine C. Histidine D. Cysteine E. Methionine 17.You have just delivered a baby whose mother had untreated PKU. Based on this it is highly likely that the following type of amino acid would be elevated in the newborn A. A nonpolar B. An uncharged polar C. A basic D. An acidic E. Branched

18.The Henderson-Hasselbalch equation may be characterized by the following? A. It determines the amount of the ionized form of a drug within the blood B. It indicates that maximal buffering occurs when [HA] >>> [A-] C. pH = pKa log [C02]/ [ HCO3 -]

7 D. pH = pKa + log [ CO2] /[ HCO3 -] E. pH = pKa + log[ HCO3 -] / [ CO2] 19.The acid titration curve for Glycine would be described by the following ? A. It would have 1 buffering region B. It would have 2 buffering region C. It would have curve similar to that of alanine D. At a point on the curve the side chain would be positively charged E. At a point on the curve the side chain would be negatively charged

20.How would you characterize valine? A. It would tend to precipitate if placed in the blood B. If placed in a hydrophobic solution it would have charge of 0 if the solution has a pH of 7 C. If placed in a hydrophobic solution it would have charge of -1 if the solution has a pH of 7 D. If placed in a hydrophobic solution it would have charge of +1 if the solution has a pH of 7 E. The side chain would lose its proton in a basic solution

21.You have decided to directly inject aspirin into your patients blood using an intravenous line of delivery. You are doing so due to a particular gastrointestinal condition. Based on this the following would be correct? A. Aspirin would mainly be uncharged B. Aspirin would mainly be negatively charged

8 C. Aspirin would mainly be positively charged D. The pKa value is determined by the property of the solution(acidic or basic) E. The formula would be pH= pKa + log [Drug-H]/[Drug-]

22.The pH of a particular tissue within the human body has a pH of 8.6. You would like to treat this area by buffering with a molecule. The molecule should have the following characteristics: A. You should focus on the alpha carboxyl group since it will do most of the buffering B. You should use a molecule which has a beta carboxyl group to assist with maxmal buffering C. You should choose a molecule whose pKa is 7.6 D. You should choose a molecule whose pKa is 6.6 E. You should choose a molecule whose pKa is 8.6

23.The letters A through E designate certain regions on the titration curve for glycine (see text). Which one of the following statements concerning this curve is correct? A. Point A represents the region where glycine is deprotonated. B. Point B represents a region of minimal buffering. C. Point C represents the region where the net charge on glycine is zero. D. Point D represents the pK of glycine's carboxyl group. E. Point E represents the pI for glycine

24.Which one of the following statements concerning the peptide shown below is correct? Gly-Cys-Glu-Ser-Asp-Arg-Cys

9 A. The peptide contains glutamine. B. The peptide contains a side chain with a secondary amino group. C. The peptide contains a majority of amino acids with side chains that would be positively charged at pH 7. D. The peptide is able to form an internal disulfide bond.