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BIO 111 Exam Notes

by: John

BIO 111 Exam Notes BIO 111

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This covers all the material involved in chapter 8 for the exam
Principles of Biology (BIO 111, Dr. Metzler)
Dr. Metzler
Study Guide
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This 2 page Study Guide was uploaded by John on Friday October 14, 2016. The Study Guide belongs to BIO 111 at Ball State University taught by Dr. Metzler in Fall 2016. Since its upload, it has received 14 views. For similar materials see Principles of Biology (BIO 111, Dr. Metzler) in Biology at Ball State University.


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Date Created: 10/14/16
Chapter 8 1. Explain the role of catabolic and anabolic pathways in cellular metabolism. a. Catabolic – breaking down of macromolecules. Energy is released (+G). b. Anabolic – building up of monomers into larger substances. Energy is used (-G). 2. Distinguish between kinetic and potential energy. a. Kinetic – energy of motion b. Potential – stored energy 3. Explain the first and second laws of thermodynamics in your own words. a. First law of thermodynamics – matter cannot be created nor destroyed. All matter that we currently have has been since the Universe was created. b. Second law of thermodynamics – the Universe is always increasing in the amount of disorder (entropy). 4. Explain why highly ordered living organisms do not violate the second law of thermodynamics. a. Organisms are open systems that are continuously taking organized energy (organic molecules) and replacing highly ordered energy in their environment with energy such as heat. 5. Write and define each component of the equation for free-energy change. a. ∆G = ∆H - T∆S b. ∆G = If this is negative, it is spontaneous. If it is positive, it is not spontaneous c. ∆H = Change in enthalpy (energy) d. T∆S = Difference in entropy multiplied by temperature. e. If enthalpy (∆H) > entropy * temperature (T∆S), energy was added to the system f. If enthalpy (∆H) < entropy * temperature (T∆S), energy has left the system 6. Distinguish between exergonic and endergonic reactions in terms of free energy change. a. Exergonic (-∆G) – free energy exits the system, spontaneous b. Endergonic (+∆G) – free energy enters the system, not spontaneous 7. Explain why metabolic disequilibrium is one of the defining features of life. a. If at equilibrium, the cell cannot do work. ∆G = 0 and the cell is dead because no work is being done 8. Describe the structure of ATP and identify the major class of macromolecules to which ATP belongs. a. Adenosine triphosphate is the phosphorylated form of ADP. ATP contains the sugar ribose, the nitrogenous base adenine, and three phosphate groups bonded to it. Used to make RNA. 9. Explain how ATP performs cellular work. a. ATP transfers energy throughout the cell. It is used as an energy source is photosynthesis and cellular respiration. Enzymes consume it and it’s used in many other things. 10. Describe the function of enzymes in biological systems. a. Enzymes host an active site for a substrate to attach to, accelerating the reaction. However, competitive inhibitors can bind to that same site and prevent the reaction from taking place. Or noncompetitive inhibitors will bind to a different part but still slow down the reaction. 11. Explain why an investment of activation energy is necessary to initiate a spontaneous reaction. a. Naturally, molecules are stable. They need enough energy to become unstable and be able to break their bonds. 12. Explain how enzyme structure determines enzyme specificity. a. Lock & key – specific enzymes work with specific molecules 13. Describe the mechanisms by which enzymes lower activation energy. a. The reaction takes place the product is created. This product is then used to slow down/end the initial reaction. 14. Explain how substrate concentration affects the rate of an enzyme-catalyzed reaction. a. The reaction rate will increase until saturation. At saturation, there’s too many substrates which results in a backup of substrate. 15. Explain how temperature, pH, cofactors, and enzyme inhibitors can affect enzymes a. Temperature – Increased temperature will increase the reaction until it is too hot so it denatures the protein b. pH – too acidic or too basic will result in denaturation c. cofactors – fit in with the substrate on the enzyme to activate/deactivate the reaction d. enzyme inhibitors – prevent the reaction from taking place by taking up the binding site 16. Describe how allosteric regulators may inhibit or stimulate the activity of an enzyme. a. allosteric regulators, such as the inhibitors and the activators, stabilizes the inactive form of the enzyme's active site and stabilizes the active forms of the functional active sites. 17. Explain how feedback inhibition prevents a cell from wasting chemical resources. a. This process takes the product of the reaction and uses it to slow down/end the initial reaction.


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