Chapter 10 Study Guide PDF

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Download Chapter 10 Study Guide PDF

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Chapter 10 Study Guide Advice: Make Flashcards for the numerous vocabulary terms. Always reference the textbook for additional information! Note: Hints are italicized in parentheses next to certain study guide questions! 1. Define catabolism and anabolism and their MAIN difference. (Hint: A for addition, C for catastrophe!) catabolism –provides energy, reducing power, precursors for biosynthesis (carbon skeletons), “breakdown” anabolism – synthesis of complex organic molecules from simpler ones, requires energy, 3 phases (biosynthesis, polymerization, assembly) “Addition or Building up” 2. Which type of cellular work involves nutrient uptake and waste elimination? (Know the other types of cellular work and their examples as well.) Transport Work involves nutrient uptake and waste elimination. Chemical Work = synthesis of complex molecules Mechanical Work = cell motility and movement of structures within cell 3. Define the laws of thermodynamics. How many are there? Law of Thermodynamics- science that analyzes energy change in a collection of matter called a system, “System + Surroundings = Universe” There are 2 Laws First – energy cannot be created nor destroyed Second – physical and chemical processes proceed in such a way that the disorder of the universe increases to the maximum possible 4. 1 calorie = 4.1840 J (What is a calorie and what is a Joule?) Calorie – amount of heat need to raise 14.5 to 15.5 Joule – units of work 5. What does the numerical value of free energy indicate? (Define endothermic and exothermic. You will see these terms on the exam.) Expresses the change in energy that can occur in chemical reactions. Exothermic – spontaneous Endothermic – nonspontaneous 6. What does it mean if (delta)G is negative? (It can mean several things…) Spontaneous, Exothermic, 7. How can you find degrees Kelvin from degrees Celsius? 273 + C 8. What does it mean if the equilibrium constant (K) is greater than one? It is mostly products 9. How many “high energy” bonds does ATP have? Explain why. *** 2 High Energy bonds because it stabilizes molecule 10. Which phosphorylated molecule has the highest phosphate transfer potential? (Define phosphate transfer potential first so you understand what the question is asking.) Which molecule has the lowest?

Phosphoenolpyruvate Phosphate Transfer Potential 11. How do you find the standard redox potential if you are given the values for the oxidizing agent and reducing agent? (There is a trick/equation for this in the powerpoints!) 12. What are the units for standard redox potential? Volts 13. What are all the other names/forms for “oxidized”? “Reduced”? How do you determine which is which in a set of half reactions, given their standard redox potential values? (Please know all the different names because they will be used interchangeably on the exam.) 14. What kind of relationship exists between (delta)E and (delta)G? Refer to their signs. They are proportional 15. Write and describe the Nernst Equation. What are the unit(s) for Faraday’s constant? 16. Does the reductant gain or lose electrons? Gains electron 17. Where does the ETC take place in a prokaryotic cell? What about for eukaryotic cells? Prokaryotes – cell membrane Eukaryotes – mitochondria or chloroplast 18. What is unique about the process of fermentation? 19. What is the role of NAD? List important electron carriers and their functions. (Dr. White mentioned that you need to know how many electrons and/or protons the carriers can hold…!!) NADH and NADPH – 2 e and 1 p FAD and FMN – 2e and 2p CoQ- 2e and 2p Cytochromes – use iron to transport 1 electron at a time Nonheme- uses iron to transport 1 electron at at time 20. What is the relationship between the proton motive force and the electron transport chain? 21. What are flavoproteins? Proteins with FAD and FMN 22. What are the three styles/types of biochemical pathways? 1. Linear 2. Branching 3. Cyclic 23. What is an electron transport molecule that ONLY transfers electrons? Cytochromes and Nonheme 24. Describe enzymes and their significance in reactions. What are the names of enzymes based on? Can enzymes alter the equilibrium of a reaction? Why or why not?

Enzymes speeds up the rate. Names are based on polypetides. Yes because they can change the activation energy. 25. What is the Michaelis constant (Km) of an enzyme? Relate it to maximum velocity of an enzyme. The substrate concentration required by the enzyme to operate at half its maximum velocity 26. What is the protein component of an enzyme? The nonprotein component? Recognize these terms. Apoenzyme, the protein component. Cofactors, the nonprotein 27. What is the active site of an enzyme? What is another name for the active site? What is activation energy? Active site- where the enzyme binds 28. Describe the two kinds of cofactors. Prosthetic – firmly attached Coenzyme – loosely attached 29. Describe the induced-fit model of enzyme-substrate interactions. How does it differ from the lockand-key model? Induced-fit model – Substrate approaches enzyme, enzyme and substrate will go through confirmation Lock and Key – Substrate (key) fits perfectly into the Enzyme (lock) 30. What is the relationship between substrate and enzyme concentration? What does saturation imply? 31. What is denaturation? What are chaperonins? Denaturation – loss of biological activity Chaperonins – protein that helps maintain protein folding 32. What is the pH inside a cell usually? 7 33. Compare and contrast competitive and noncompetitive inhibition. Give examples of each. Competitive- competes with binding site. Noncompetitive – binds to another site, changes enzyme shape 34. Define ribozymes. Where did we hear about this before?? What are some examples of their roles in cells? Where are they often located? Doesn’t need protein. RNA, translation, splicing, self-replication 35. What are the three major mechanisms of metabolic regulation? What are some reasons for metabolic regulation? What are examples of post-translational regulation mechanisms? Metabolic Channeling (compartmentation) Regulation of the synthesis of a particular enzyme (translational) Direct Stimulation or inhibition of the activity of a critical enzyme (post-translational) 36. Describe the process of metabolic channeling.

37. How do effector molecules bind in allosteric regulation? Define allosteric regulation. Describe positive/negative allosteric effectors. 38. What is unique about covalent modification of enzymes? What groups are they involved with? (Remember MAP or PAM!!) 39. Define feedback inhibition. What is an alternate name for the process? How are isoenzymes significant to the process? What are pacemaker enzymes? 40. Describe the cellular significance of ATP, beyond just simple “energy”. BONUS: Your exam may include at least one electrochemical math problem involving Nernst Equation, half reactions, finding deltaG/deltaE, and identifying if a reaction is exothermic/endothermic. Webcourses, your SARC tutor, and your SI leader have posted Electrochemical math problems you can solve for practice! Please make sure you can solve those....