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






3. What stabilizes lipid bilayer?






4. 3 carbon triol that forms backbone of triacylglycerol






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






6. 4 causes of denaturation of proteins






7. Characteristics of acidic amino acids






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






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






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






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






12. Characteristic of basic amino acids






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






14. Sulfur containing amino acids






15. Energy storage molecule of carbohydrates for plants






16. 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)






17. 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






18. Acetic acid formula?






19. Unique feature of glycine






20. Fatty acid structure






21. Interconversion btw two anomers






22. D and L describe what?






23. Sugar with an aldehyde at the first carbon position






24. Basic amino acids






25. Characteristics of hydrophobic amino acids






26. Polar amino acids






27. Nonpolar - hydrophobic amino acids






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






29. 2 things that accelerate the rate of hydrolysis for peptide cleavage?






30. Glycosidic linkage of lactose






31. Naturally occurring carbohydrates are formed from what?






32. Unique feature of cysteine






33. Characteristics of polar amino acids






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






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






36. Glyceraldehyde






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






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






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






40. Fxn of cholesterol in the membrane?






41. Hydrophilic amino acids






42. Molecules with the same atoms - but different bonds






43. Formula for urea






44. Glycosidic linkage of cellulose






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






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






47. 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






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






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






50. 2 covalent bonds formed in proteins