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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 cell to another
4. What are the functional groups common to all amino acids? ANS amine and carboxylic acid
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,
- 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 the N-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 polypeptide chain. Quaternary structure is the orientation of multiple subunits.
10. Proteins typically adopt either a conformation that is fibrous or
. ANS globular
11. What is the function of an enzyme? ANS to accelerate the rate of a biological reaction
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 inhibitor binds 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
18. polar amino acids properties ANS -contain side chains that have a dipole, and most 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
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 10,000 g/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
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
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 transition state
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
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 reacts with 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
61. term used to describe the chemistry of large compounds ANS supramolecular chemistry
