Review Sheet

Attachments:5 Added by Michael Evans, last edited by Michael Evans on Apr 06, 2012 (view change)

General advice:
1. Enter the exam room with a strategy. For example, it's more important to answer all the questions correctly than it is to get them correct on the first try so take some risks. Don't be discouraged by incorrect responses (there are a lot of residual points on this test). 2. Bring some swagger with you. Stay cool. You've prepared; you're ready to think; you'll prevail. 3. Put on your favorite tunes and get in the zone (you're allowed to wear earbuds during the exam but respect your neighbor and keep the volume low). 4. Practice the mock exams under mock conditions. Set the timer and take them in a place that is free of distractions. 5. Be skilled with ACE. Practice using the ACE shortcut keys. Watch the other ACE instructional videos and do the tutorials if the ACE graphical user interface is not "second nature" to you. Know how to copy and paste structures efficiently in ACE. 6. Be able to draw curved arrows in ACE for reaction mechanisms. Always pay attention to the atoms that will be connected as indicated by the blue dashed lines and parentheses. Note: For enlarged working space, open a "B-A" Sketcher Window (View -> Sketcher Window). 7. Be able to communicate stereochemistry to ACE (i.e., R/S configurations of sp3 centers AND E/Z configurations of double bonds). Tip: always turn on R/S labels and E/Z labels before you submit an answer, just to be sure that ACE is correctly interpreting your stereochemistry. 8. Knowing the nodal patterns for linear n-atom pi-systems (e.g., n=2 through n=6) will help you solve problems faster; draw them out ahead of time and understand them. 9. Be skilled using SHMO. Given a complex molecule, know how to add only the relevant atoms into a SHMO calculation. Do the Aromaticity & Cyclical Pi MOs POTDs. 10. You must know how to interpret MOs (e.g., from WebMO). If a problem requires a WebMO calculation the results will be provided for you (in other words, no problem on the exam will require you to do a WebMO calculation, but you are allowed to use WebMO if it will help you solve a problem). 11. Review the elementary steps as summarized in Frontier Molecular Orbital Theory notes and the CHEM 232 Webcasts; specifically, pt (15.2), DN, AN, SN2 (18.2), DE, Ebeta (19.2), E2 (19.3), 1,2R (21.2), AE (24.1), AdN (28.1), Ebeta (29.2). Be able to use elementary steps to help you work through problems. 12. Make sure you don't spend too much time on any one question. Make a plan as to how you'll navigate through the exam, and what you'll do when you hit a wall. For example: I'll spend no more than 6 min. on any one problem. Once I've attempted a problem so many times that it's reached its residual value, it's time to move on. I'll return to this problem only after the other problems are finished. If I get stuck I will look ahead because it may be helpful to work some problems backwards.

Specific study tips:

1. Recognize the anomeric position of sugars as a good electrophile. Consider the likely reactivity of sugar phosphates in the presence of nucleophiles, such as other sugars. Be able to predict the products of these substitution reactions. 2. Have the ability to identify the stereotopic relationship between two groups in a molecule. Have the ability to identify the stereotopic relationship between two faces of one or more planar groups (check out #3-6 in the Enzyme Stereochemistry POTDs). Be able to carry out the Q test using deuterium (D) and R/S Labels in ACE. 3. Understand dehalogenation reactions that operate via radical mechanisms. Be able to draw a mechanism for the initiation phase of a dehalogenation reaction (which is consistent with initiations of other radical reactions, as well). 4. When given the propagation mechanism of a radical reaction, be able to enumerate all of the reaction's possible termination products. 5. Understand the stability trends of radicals and how bond dissociation energy influences the likelihood of radical formation. 6. Understand the concept of temporary intermolecularity, the covalent attachment of a catalyst to a substrate and subsequent general acid or base assistance. Read the short perspective here for an introduction to this concept. Be able to draw a mechanism for formation of the key catalytic intermediate, which contains a general acid or base in an ideal position to catalyze an elementary step in an intramolecular way. 7. Be able to name the heterotopic faces of a planar group using the Re/Si convention. Given the configuration of a new stereocenter formed from a prochiral group, be able to identify which face (Re/Si) reacted to form that product. 8. Have the ability to trace atoms throughout a biosynthetic pathway, and map the atoms of a compound onto those of a distant metabolite by following them through multiple chemical transformations. 9. Understand the dependence of major ionization state on pH. Be able to utilize given pKa's and pH's to predict the dominant ionization state of a compound at the given pH. 10. Read the Science article associated with problems on the mock exam and on the exam itself. Reading the full article requires you to be on campus or use a VPN connection. 11. Consider the mechanisms described in the Science article. Be able to draw these mechanisms using the elementary steps that we have discussed throughout CHEM 232 and 332. Understand general acid/base catalysis, and consider how general acids and bases in the form of amino acid side chains may get involved in each elementary step. 12. Given the reaction carried out by an enzyme on its natural substrates, be able to draw the product of an analogous reaction between an inhibitor and one of the natural substrates. Specifically, consider sulfa inhibitors and dihydropteroate synthase (from the Science article). 13. Be able to determine the stereochemical outcome of a reaction based on a threedimensional model resembling its transition state. Consider the E/Z configuration of double bonds, retention/inversion of configuration at tetrahedral carbons, and R/S labels. 14. Understand the meaning of kobs (or kcat) and Km. Be able to interpret a collection of kobs and Km values to pinpoint mutations that affect the rate of an enzyme and/or binding affinity of the substrate(s) for the enzyme. Add Labels Add Comment