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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. (+) and (-) describe what?






2. Sulfur containing amino acids






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






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






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






6. Characteristics of acidic amino acids






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






8. 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






9. Polar amino acids






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






11. Characteristics of hydrophobic amino acids






12. 2 things that accelerate the rate of hydrolysis for peptide cleavage?






13. D and L describe what?






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






15. Molecules with the same atoms - but different bonds






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






17. 4 causes of denaturation of proteins






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






19. 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






20. Physiological pH






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






22. 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)






23. Hydrophilic amino acids






24. Formula for urea






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






26. Fxn of cholesterol in the membrane?






27. Acetic acid formula?






28. Basic amino acids






29. Interconversion btw two anomers






30. 3 physiological roles of lipids






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






32. Sugar with an aldehyde at the first carbon position






33. Glycosidic linkage of maltose






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






35. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule






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






37. Characteristic of basic amino acids






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






39. Histidine






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






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






42. Hydrolysis






43. Unique feature of cysteine






44. Name for 6 membered ring






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






46. Energy storage molecule of carbohydrates for animals






47. What stabilizes lipid bilayer?






48. 3 carbon triol that forms backbone of triacylglycerol






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






50. Unique feature of proline