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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. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled






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






3. Characteristics of hydrophobic amino acids






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






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






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






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






8. Interconversion btw two anomers






9. Characteristic of basic amino acids






10. What kind of lipids compromise the lipid bilayer?






11. Naturally occurring carbohydrates are formed from what?






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






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






14. Enzyme that hydrolyzes maltose into 2 glucose molecules?






15. Glycosidic linkage of cellulose






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






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






18. Glyceraldehyde






19. Characteristics of polar amino acids






20. Energy storage molecule of carbohydrates for plants






21. Basic amino acids






22. Unique feature of cysteine






23. Glycosidic linkage of sucrose






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






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






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






27. 2 covalent bonds formed in proteins






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






29. Sugar with an aldehyde at the first carbon position






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






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






32. Hydrolysis






33. Characteristics of acidic amino acids






34. Hydrophilic amino acids






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






36. 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






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






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






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






40. 3 carbon triol that forms backbone of triacylglycerol






41. Formula for urea






42. Glycosidic linkage of lactose






43. Molecules with the same atoms - but different bonds






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






45. 4 causes of denaturation of proteins






46. What stabilizes lipid bilayer?






47. Enzymes that hydrolyze fats






48. Histidine






49. 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






50. 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)