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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. Histidine






2. 3 physiological roles of lipids






3. Glycosidic linkage of maltose






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






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






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






7. Hydrophilic amino acids






8. 2 covalent bonds formed in proteins






9. Unique feature of proline






10. What kind of lipids compromise the lipid bilayer?






11. 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)






12. Enzyme that hydrolyzes lactose into galactose and glucose into






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






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






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






16. 3 carbon triol that forms backbone of triacylglycerol






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






19. Diastereomers that vary in the configuration of 1 chiral center






20. Hydrolysis






21. Basic amino acids






22. 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






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






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






25. Characteristic of basic amino acids






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






27. Naturally occurring carbohydrates are formed from what?






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






29. Glycosidic linkage of lactose






30. What stabilizes lipid bilayer?






31. D and L describe what?






32. Interconversion btw two anomers






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






34. Molecules with the same atoms - but different bonds






35. 2 things that accelerate the rate of hydrolysis for peptide cleavage?






36. Enzyme that hydrolyzes maltose into 2 glucose molecules?






37. Energy storage molecule of carbohydrates for animals






38. 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






39. Name for 5 membered ring






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






41. Unique feature of cysteine






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






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






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






45. Unique feature of glycine






46. Glycosidic linkage of sucrose






47. Nonpolar - hydrophobic amino acids






48. Glyceraldehyde






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






50. 4 causes of denaturation of proteins