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






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






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






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






5. Molecules with the same atoms - but different bonds






6. Sulfur containing amino acids






7. Basic amino acids






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






9. 3 carbon triol that forms backbone of triacylglycerol






10. D and L describe what?






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






12. Glycosidic linkage of lactose






13. Physiological pH






14. Histidine






15. Acidic amino acids






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






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






18. 4 causes of denaturation of proteins






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






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






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






22. What stabilizes lipid bilayer?






23. Characteristics of hydrophobic amino acids






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






25. 2 things that accelerate the rate of hydrolysis for peptide cleavage?






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






27. Name for 6 membered ring






28. Sugar with an aldehyde at the first carbon position






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






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






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






32. Hydrophilic amino acids






33. 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






34. Formula for urea






35. Glycosidic linkage of maltose






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






37. Acetic acid formula?






38. Fatty acid structure






39. 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






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






41. Enzyme that hydrolyzes lactose into galactose and glucose into






42. Hydrolysis






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






44. 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






45. Energy storage molecule of carbohydrates for animals






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






47. Unique feature of cysteine






48. 3 physiological roles of lipids






49. Unique feature of glycine






50. Nonpolar - hydrophobic amino acids