CHEM 210 Module 3 Exam Newest

1. Name three different functions of proteins. ANS Transport, hormones,

catalysis,structure, and protection

2. What function does a protease have? ANS catalysis. It degrades proteins.

3. What is the function of hormones? ANS These proteins communicate from

one cellto another

4. What are the functional groups common to all amino acids? ANS

amine andcarboxylic acid

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5. Briefly describe the five major groupings of amino acids. ANS The amino

acids are grouped into 1) nonpolar, aliphatic 2) nonpolar and aromatic 3) polar but

neutral,

4) acidic, and 5) basic.

6. What amino acid can form a disulfide bond? ANS Cysteine

7. Which amino acid is the only one to have its side chain connected to the

amine group? ANS proline

8. Consider the following pentapeptide ETYLVD.

Which amino acid is at the N terminal? Which is at the C terminal? ANS E is

at theN-terminal, and D is at the C-terminal.

9. Differentiate between protein tertiary structure and protein quaternary

structure. ANS Tertiary structure is the conformation or shape of a single

polypeptidechain. Quaternary structure is the orientation of multiple subunits.

10. Proteins typically adopt either a conformation that is fibrous or

11. What is the function of an enzyme? ANS to accelerate the rate of a

biologicalreaction

12. How does a competitive inhibitor differ from a uncompetitive inhibitor?

ANS A competitive inhibitor binds at the active site of the enzyme. An uncompetitive

inhibitorbinds at a site distinct from the active site, but it still inhibits the enzyme.

13. What three factors influence enzyme catalyzed reactions? ANS pH,

tempera-ture, and concentration of enzyme and substrate

14. The 20 side chains differ in ANS composition, size, and charge

15. Aliphatic amino acids properties ANS -relatively small, which permits

them to interact with other groups. --found in the interior of the protein, away

from water,nestled with other aliphatic groups

16. unique function of proline ANS -structure of proline is not flexible, which

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is anadvantage (and disadvantage) in protein structure.

17. non-polar aromatic group properties ANS -side chains of these compounds

con-tain a ring of carbons as an aromatic functional group

-These groups are not as small as the aliphatic, but they are more rigid.

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18. polar amino acids properties ANS -contain side chains that have a

dipole, andmost can hydrogen bond

- interact strongly with water

19. two cysteines together form ANS disulfide bonds by their sulfur atoms

20. dipole bonds common in ANS keratin proteins found in hair cells

21. Amino acids can be joined together into long chains called ANS

polypeptides

22. The reaction to two amino acids to form a dipeptide with a peptide bond

ANS -

peptide bond formation

23. used to describe a short chain of amino acids usually from two to twenty

amino acids ANS oligopeptide

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24. After 100 residues have been added together, it is said that the molecule

has attained the status of a ANS protein

25. When a protein has 100 amino acids, the protein mass is about ANS

10,000g/mol

26. is the term used to describe the chemistry of large compounds. ANS

Supramol-ecular chemistry

27. Portions of proteins may exist in a random conformation, or, as they are

often called ANS intrinsically disordered.

28. refers to the order of amino acids covalently bonded together, including

disulfide bonds, in a polypeptide chain. ANS Primary structure

29. There are three types of secondary structure ANS (1) alpha-

helices, (2)beta-sheets, and (3) beta turns

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30. coiled structures of amino acids where the backbone atoms form hydrogen

bonds to stabilize this sequence. ANS Alpha-helices

31. proteins that accelerate the speeds of chemical reactions ANS enzymes

32. are the chemical species that bind to the enzyme and are converted to

another compound. ANS substrate

33. the enzyme, acts to break the double bond of the substrate by adding water

across the double bond ANS fumarase

34. which is a class of enzymes that creates double bonds or adds molecules

to double bonds. ANS lyases

35. catalyze oxidation and reduction reactions ANS Oxidoreductases

36. catalyze the transfer of a group from one molecule to a second ANS

transferals

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37. catalyze the breaking, or hydrolysis, of bonds ANS hydrolases

38. catalyze the forming or breaking of double bonds ANS lyases

39. catalyze the rearrangement within a single molecule ANS isomerases

40. catalyzes the joining of two molecules, or two parts of a molecule ANS

ligases

41. Some enzymes, including fumarase, have non-protein components ANS

cofac-tors

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42. Organic compounds function as cofactors as well, and when they do, they

are called ANS coenzymes

43. examples of coenzymes ANS vitamin c and niacin

44. an enzyme without the co-factor (either ion or coenzyme) is called an ANS

apoenzyme

45. When the cofactor is added to the apoenzyme to produce a functional

enzyme, this called ANS holoenzyme

46. which is the small movements of amino acids in the enzyme to bind

specifically to the substrate ANS induced fit

47. the structure of the molecule in its transition into a new molecule ANS

transitionstate

48. Too much of an increase in temperature can cause a protein to lose its

active conformation, ANS unfolding

49. can slow down or stop enzyme reactions. ANS inhibitors

50. bind at a spot distinct from the active site and prevent catalysis from taking

place. ANS uncompetitive inhibition

51. compete with the natural substrate for the active site. ANS competitive

inhibitor
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52. can bind either to the lone enzyme or the enzyme-substrate complex.

ANS -

mixed inhibitor

53. which is a four-residue unit that turns 180o degrees ANS beta turn

54. Collections of particularly stable groups of secondary structures are often

referred to as ANS motif

55. which is a non-amino acid portion of the molecule necessary for the

structure and function of the protein. ANS prosthetic group

56. describes macromolecules that have two or more independent polypeptide

chains that associate with one another. ANS quarternary structure

57. proteins that contain two polypeptides ANS dimer

58. one oxygen from the carboxylic acid group and two hydrogens from the

amino group are lost as water, which is called ANS condensation reaction

59. how to form peptide bond ANS -amino functional group of one amino acid

reactswith the carboxylic acid functional group of a second.

-The result is that the two monomers are joined together, producing a dipeptide with

the release of water

60. how does a dipeptide continue to grow ANS amino acids added to carboxy

end

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61. term used to describe the chemistry of large compounds ANS

supramolecularchemistry

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