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MCAT Organic Chemistry 2

Subjects : mcat, science
Instructions:
  • Answer 50 questions in 15 minutes.
  • If you are not ready to take this test, you can study here.
  • Match each statement with the correct term.
  • Don't refresh. All questions and answers are randomly picked and ordered every time you load a test.

This is a study tool. The 3 wrong answers for each question are randomly chosen from answers to other questions. So, you might find at times the answers obvious, but you will see it re-enforces your understanding as you take the test each time.
1. Amino group placed on the left of a fischer projection is a?






2. (R) and (S) describe what?






3. Generated btw either thiols on different proteins or thiols on the same protein






4. 3 carbon triol that forms backbone of triacylglycerol






5. Characteristic of basic amino acids






6. Molecules with the same atoms - but different bonds






7. 1. it exists in solution in equilibrium with linear form 2. mutarotation occurs readily 3. it is a reducing sugar - and reacts positively w/ Benedict's reagent






8. Enzyme that hydrolyzes maltose into 2 glucose molecules?






9. Polar amino acids






10. Right handed helix w/ carboxyl of one amino acid bound to the amine of another amino acid three residues away - proline never resides in this structure b/c it would place a kink in the helix






11. Unique feature of proline






12. What kind of lipids compromise the lipid bilayer?






13. Fatty acid w/ no double bonds and maximum number of hydrogens






14. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain






15. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone






16. Acidic amino acids






17. Property of fatty acids where one end is hydrophobic and the other is hydrophilic






18. Formula for urea






19. Unique feature of cysteine






20. Naturally occurring carbohydrates are formed from what?






21. What describes the affinity of functional groups for a proton?






22. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond






23. Characteristics of hydrophobic amino acids






24. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode






25. Hydrolysis






26. Physiological pH






27. Sugar with a carbonyl group at the 2 carbon position






28. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test






29. Fatty acid w/ one or more double bonds in cis form predominately






30. PH at which positive and negative charges balance to form a zwitterion






31. Interaction btw polypeptide subunits arranged in polypeptide. can be covalent bonds or intermolecular forces - disulfide bond that does not form btw residues on the same protein affect (blank)






32. Energy storage molecule of carbohydrates for plants






33. Interconversion btw two anomers






34. Glycosidic linkage of sucrose






35. Diastereomers that vary in the configuration of 1 chiral center






36. Sugar with an aldehyde at the first carbon position






37. Name for 5 membered ring






38. Enzyme that hydrolyzes lactose into galactose and glucose into






39. Nonpolar - hydrophobic amino acids






40. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure






41. 4 causes of denaturation of proteins






42. Basic amino acids






43. Glyceraldehyde






44. The amino acid sequence of a protein that is determined by peptide bond






45. 2 reasons why fats have more efficient energy stores than carbs






46. Enzymes that hydrolyze fats






47. 2 covalent bonds formed in proteins






48. 2 things that accelerate the rate of hydrolysis for peptide cleavage?






49. Epimers of sugars that vary in the configuration of their anomeric carbons






50. 3 physiological roles of lipids