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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. 2 covalent bonds formed in proteins






2. Molecules with the same atoms - but different bonds






3. Glycosidic linkage of lactose






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






5. 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






6. Amino group placed on the right of a fischer projection is a?






7. What configuration do all naturally occuring amino acids have?






8. Amino group placed on the left of a fischer projection is a?






9. What stabilizes lipid bilayer?






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






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






12. Unique feature of glycine






13. What kind of lipids compromise the lipid bilayer?






14. Fxn of cholesterol in the membrane?






15. D and L describe what?






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






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






18. 4 causes of denaturation of proteins






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






20. 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)






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






22. Polar amino acids






23. Physiological pH






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






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






27. Hydrolysis






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






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






30. Unique feature of cysteine






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






32. Acidic amino acids






33. Hydrophilic amino acids






34. Nonpolar - hydrophobic amino acids






35. Characteristic of basic amino acids






36. Unique feature of proline






37. 2 reasons why fats have more efficient energy stores than carbs






38. Energy storage molecule of carbohydrates for animals






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






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






41. Characteristics of polar amino acids






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






43. Enzymes that hydrolyze fats






44. Histidine






45. Naturally occurring carbohydrates are formed from what?






46. Characteristics of hydrophobic amino acids






47. Basic amino acids






48. Glycosidic linkage of sucrose






49. 3 physiological roles of lipids






50. Name for 5 membered ring