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






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






3. Characteristic of basic amino acids






4. Formula for urea






5. Characteristics of acidic amino acids






6. PH at which the amino acid has a net neutral charge






7. 3 carbon triol that forms backbone of triacylglycerol






8. (+) and (-) describe what?






9. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure






10. Enzyme that hydrolyzes lactose into galactose and glucose into






11. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal






12. Name for 5 membered ring






13. Hydrolysis






14. Nonpolar - hydrophobic amino acids






15. Glycosidic linkage of lactose






16. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled






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






18. Hydrophilic amino acids






19. Basic amino acids






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






21. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?






22. Characteristics of polar amino acids






23. Sulfur containing amino acids






24. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids






25. Covalent bond formed btw carboxyl group of one atom and the amino group of another amino acid in an addition - elimination mechanism - enzymes are required to carry out rxn






26. Glycosidic linkage of cellulose






27. Acidic amino acids






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






29. Polar amino acids






30. Unique feature of proline






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






32. 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)






33. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers






34. Name for 6 membered ring






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






36. 2 reasons why fats have more efficient energy stores than carbs






37. Glycosidic linkage of sucrose






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






39. 2 things that accelerate the rate of hydrolysis for peptide cleavage?






40. Fatty acid structure






41. Histidine






42. What kind of lipids compromise the lipid bilayer?






43. D and L describe what?






44. 2 covalent bonds formed in proteins






45. 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






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






47. Enzyme that hydrolyzes maltose into 2 glucose molecules?






48. Interconversion btw two anomers






49. Glycosidic linkage of maltose






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