Final_exam_review - Biochemistry 3304 Review Legge I. True...

Info iconThis preview shows pages 1–4. Sign up to view the full content.

View Full Document Right Arrow Icon
Biochemistry 3304 Review Legge I. 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 F 7. 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 FADH 2 . T F 9 Michaelis-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. Calculations The 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 SDS A. 4.5 B. 0.0045 g SDS C. 4.5 kg SDS D. 4.5 mg SDS E. 4.5 g SDS 12. 20 % SDS A. 446 g SDS B. 446 mg SDS C. 20 g SDS D. 20 mg SDS E. 2.0 g SDS 13. 20 mg/ml SDS A. 2.0 g SDS B. 2.0 mg SDS C. 4.5 mg SDS D. 0.45 mg SDS E. 4.5 g SDS
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Biochemistry 3304 Review Legge III. Matching Below 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. ________ 14. The dashed line representing an increase in the pH of the hemoglobin solution. ________ 15. The dashed line representing the oxygen binding curve of myoglobin. 1.0 0.75 0.5 0.25 Increasing pO 2 (torr) A Y O 2 1.0 0.75 0.5 0.25 Increasing pO 2 (torr) B Y O 2 1.0 0.75 0.5 0.25 Increasing pO 2 (torr) C Y O 2 1.0 0.75 0.5 0.25 Increasing pO 2 (torr) D Y O 2 1.0 0.75 0.5 0.25 Increasing pO 2 (torr) E Y O 2
Background image of page 2
Biochemistry 3304 Review Legge IV. 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 their molecular weights and pI’s. Your thesis advisor gave you the opportunity to name them since you discovered them. You think hard about what you want to name them and decide you will name them after your favorite mentors and teachers. You prepare a table in alphabetical order of each protein’s name to organize your new proteins and their characteristics as follow: Protein Name Molecular Weight (kDa) pI Protein “Briggs” 100 5.0 Protein “Fox” 250 10.0 Protein “Legge” 80 6.8 Protein “Tu” 15 4.5 Protein “Yeo” 45 9.5 16. Your thesis advisor asks you to go back and do another purification to isolate more of your proteins for characterization. You decide to try and change the conditions to optimize purification. The first column that you decide to try is a DEAE-cellulose column which is
Background image of page 3

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Image of page 4
This is the end of the preview. Sign up to access the rest of the document.

This note was uploaded on 07/20/2010 for the course BCHS BCHS 3304 taught by Professor Legge during the Fall '09 term at University of Houston.

Page1 / 11

Final_exam_review - Biochemistry 3304 Review Legge I. True...

This preview shows document pages 1 - 4. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online