BIO1330 Exam 2 Review Slides Fall 2024 PDF

10/7/24 Exam 2 study slides Proteins, Energy & Enzymes Fall 2024 Content from Exam 1 Cell Structure & Organelle Function as it relates to protein structure & function – Where does all this happen? Ionic, Polar covalent...

10/7/24 Exam 2 study slides Proteins, Energy & Enzymes Fall 2024 Content from Exam 1 Cell Structure & Organelle Function as it relates to protein structure & function – Where does all this happen? Ionic, Polar covalent and non-polar covalent bonds as it relates to protein structure & function – What types of bonds enable Primary, Secondary, Tertiary & Quaternary Protein Structure? Cell Membranes – as it relates to protein structure & function – How are proteins hydrophobic/hydrophilic & how does this inform us as to which parts of proteins are inside/outside of cell membranes? 1  10/7/24 Learning Objectives 1. Draw and describe the structure of an amino acid, including the central carbon, carboxyl group, amino group, and side chain. Example Question: Identify each of the three on these molecules: Learning Objectives 2. Predict whether a side chain is nonpolar, polar uncharged, or polar charged. Example Question: Categorize each of these molecules 2  10/7/24 Learning Objectives 3. Contrast hydrolysis and condensation reactions. Example question: Which are endothermic, anabolic and form polymers from monomers? Work together to solve Learning Objectives 3. Contrast hydrolysis and condensation reactions. Example question: Which are endothermic, anabolic and form polymers from monomers? Condensation reactions are endothermic & anabolic forming polymers (from monomers) by removing water Hydrolysis reactions are exothermic & catabolic using water to split monomers off polymers 3  10/7/24 Learning Objectives 4. Define the primary structure of a protein and identify and locate the peptide bonds that maintain primary structure. Which atoms will form a peptide bond? Talk amongst yourselves Learning Objectives 4. Define the primary structure of a protein and identify and locate the peptide bonds that maintain primary structure. Which atoms will form a peptide bond? 4  10/7/24 Learning Objectives 5. Identify and contrast two types of secondary structure and identify the interactions that stabilize these structures. What are the structures & what are the bonds that hold it together? Discuss: Learning Objectives 5. Identify and contrast two types of secondary structure and identify the interactions that stabilize these structures. Hydrogen bonds among atoms of the backbone 5  10/7/24 Learning Objectives 6. Identify the level of protein structure that determines the three dimensional shape of a protein and list four types of interactions that contribute to this level of structure. What are the 4 categories of bonds and what part of the amino acid is doing the binding? Learning Objectives 6. Identify the level of protein structure that determines the three dimensional shape of a protein and list four types of interactions that contribute to this level of structure. All types of bonds and interactions among the side chains of amino acids 6  10/7/24 Learning Objectives 7. Define the quaternary structure of a protein. How is quaternary defined? And what are the bonds? Work together to answer these questions. Learning Objectives 7. Define the quaternary structure of a protein. All types of bonds and interactions among the side chains of amino acids 7  10/7/24 Learning Objectives 8. Discuss the role of chaperone proteins in protein folding. Learning Objectives 8. Discuss the role of chaperone proteins in protein folding. What do they do? Where does this occur? Decide amongst yourselves 8  10/7/24 Learning Objectives 8. Discuss the role of chaperone proteins in protein folding. Tertiary & Quaternary structure Inside Er Learning Objectives 9. Predict the potential consequence to protein function if the primary structure of the protein is altered. Work together to recall some examples from lecture/worksheet – be specific 9  10/7/24 Learning Objectives 9. Predict the potential consequence to protein function if the primary structure of the protein is altered. Change in structure might = change in function Learning Objectives 10. Define and differentiate between potential energy and Gibb’s free energy. Working together, define each 10  10/7/24 Learning Objectives 11. Define and contrast endergonic and exergonic reactions with respect to changes in Gibb’s free energy. Working together, classify each below and explain your rational Learning Objectives 12. Define and contrast anabolic and catabolic reactions and give an example of each. What are some examples? 11  10/7/24 Learning Objectives 13. Correlate the following terms and describe how they relate to each other: endergonic/exergonic, anabolic/catabolic, condensation/hydrolysis. Tell me what to draw on each side-board Learning Objectives 14. Identify the activation energy, change in free energy (ΔG), and transition state on a graph of the free energy change of a reaction. Identify for me A, B & C 12  10/7/24 Learning Objectives 15. Identify whether a reaction is endergonic or exergonic using a graph of the free energy change of a reaction. Talk together to come up with what I did with this slide that differs from previous slides? Learning Objectives 16. Draw how a graph of the free energy change of a reaction is altered in the presence of an enzyme and describe the effect on the rate of the reaction and overall change in free energy (ΔG) of the reaction. Which of A, B or C does enzymes alter? 13  10/7/24 Learning Objectives 17. Identify the location of an active site on an enzyme and explain its role in facilitating reactions. Which of the above is endergonic/exergonic? Learning Objectives 17. Identify the location of an active site on an enzyme and explain its role in facilitating reactions. Which of the above is ΔG negative/positive? 14  10/7/24 Learning Objectives 17. Identify the location of an active site on an enzyme and explain its role in facilitating reactions. Which of the above is anabolic/catabolic? 18. Contrast allosteric inhibition versus competitive inhibition & define negative feedback inhibition. 15  10/7/24 Learning Objectives 19. Predict how alterations in enzyme shape could affect enzyme function. What two types of alterations have we talked about? Discuss Learning Objectives 19. Predict how alterations in enzyme shape could affect enzyme function. Primary protein structure (mutations) Regulation (allosteric = temporary shape changes) 16  10/7/24 Learning Objectives 20. Predict the potential consequence of a nonfunctional enzyme for a cell. Learning Objectives 21. Describe the role of cofactors and coenzymes in enzyme function and contrast their structures. Which are which? 17  10/7/24 Learning Objectives 21. Describe the role of cofactors and coenzymes in enzyme function and contrast their structures. 18