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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. Characteristics of hydrophobic amino acids






2. Glyceraldehyde






3. Energy storage molecule of carbohydrates for animals






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






5. Characteristics of polar amino acids






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






7. What stabilizes lipid bilayer?






8. Formula for urea






9. Name for 5 membered ring






10. Physiological pH






11. Molecules with the same atoms - but different bonds






12. Interconversion btw two anomers






13. Name for 6 membered ring






14. Glycosidic linkage of maltose






15. Sulfur containing amino acids






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






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






18. Characteristics of acidic amino acids






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






20. 2 reasons why fats have more efficient energy stores than carbs






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






22. 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






23. Glycosidic linkage of sucrose






24. Enzyme that hydrolyzes maltose into 2 glucose molecules?






25. Energy storage molecule of carbohydrates for plants






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






27. Glycosidic linkage of cellulose






28. 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)






29. Acidic amino acids






30. 2 covalent bonds formed in proteins






31. 2 things that accelerate the rate of hydrolysis for peptide cleavage?






32. D and L describe what?






33. Histidine






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






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






36. 3 physiological roles of lipids






37. Enzyme that hydrolyzes lactose into galactose and glucose into






38. Molecule can act as a base and as an acid






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






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






41. Hydrophilic amino acids






42. Acetic acid formula?






43. What kind of lipids compromise the lipid bilayer?






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






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






46. Nonpolar - hydrophobic amino acids






47. Unique feature of proline






48. 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






49. Unique feature of cysteine






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