Campbell 5.4 Reading Quiz: Proteins!
This reading quiz covers section 5. 4 in your Campbell textbook as well as some review questions on Macromolecules. If you need help on the Macromolecule questions please refer back to sections 5. 1-5. 3 in your textbook. The quiz will mostly highlight information about Proteins - especially their structures and functions as enzymes.
- 1.On the bottom of p.80 your text states that, "a protein is not just a polypeptide chain". So what is a protein? Answers will NOT be counted correct unless they are in your own words - look on p.80 for this specific spot for the best answer.
- 2.Explain what Fig. 5.19 is showing IN YOUR OWN WORDS.
- 3.List 4 things that can cause a protein to become denatured.
- 4.What happens if proteins are created with an incorrect shape?
- 5.What is the name of the process that joins monomers together to make polymers?
- A.
Hydrolysis
- B.
Monomerization
- C.
Protein formation
- D.
Coiling
- E.
Dehydration synthesis
- 6.In hydrolysis, __________________ , and in this process water is _________________________ .
- A.
A polymer breaks up to form monomers ... consumed
- B.
A monomer breaks up to form polymers ... produced
- C.
Monomers are assembled to produce a polymer ... consumed
- D.
Monomers are assembled to produce a polymer ... produced
- E.
A polymer breaks up to form monomers ... produced
- 7.In science knowing Latin and Greek roots is frequently helpful in understanding definitions. One example is hydrolysis because hydro- refers to water and -lysis means __________________ which is literally what happens during the process of hydrolysis.
- 8.Figure 5.15 in your textbook shows 8 of the possible functions of proteins in living things. In each of the 8 smaller pictures (except structural proteins), the proteins are shown in the color _________________________.
- 9.Check any of the following that are possible functions of proteins. Consult Fig. 5.15 in your text for help.
- A.
Transporting substances in/out of cells.
- B.
As a support protein in hair, feathers, connective tissues, etc.
- C.
As hormones that cause other tissues to respond.
- D.
As amino acids that make polypeptides.
- E.
As enzymes that speed up chemical reactions.
- 10.The major parts of an amino acid are a central Carbon atom, an amino group, a carboxyl group, a single Hydrogen atom, and an R group which is identical in all 20 amino acids.
- A.
True
- B.
False
- 11.According to Fig. 5.16 in your textbook, amino acids can be divided into 3 major categories based on their properties. These categories are _______________, polar, and electrically charged.
- 12.Using Fig. 5.16 in your textbook you can see that molecules that are polar are also considered ______________________, or water loving.
- 13.Every time a peptide bond is created to link 2 amino acids together a ______________ molecule is released. (See Fig. 5.17 for help)
- 14.In Fig. 5.17 in your textbook, how many amino acids are shown linked together in the molecule in the lower half of the diagram?
- A.
1
- B.
2
- C.
3
- D.
4
- E.
5
- F.
6
- 15.Every protein (polypeptide) has a free ________________ on one end and a free ___________________ on the other end.
- A.
Carboxyl group......R group
- B.
Amino group.....carboxyl group
- C.
C-terminus........C-terminus
- D.
A-terminus.......A-terminus
- 16.A polypeptide is the same as a protein.
- A.
True
- B.
False
- 17.What determines the 3-D structure that a protein will have?
- A.
Globular protein associations with amino acids
- B.
Fibrous protein associations with amino acids
- C.
The amino acid sequence of the protein
- D.
Whether the protein contains electrically charged amino acids
- 18.Fig. 5.18(a) shows the way that 1 polypeptide chain folds in 3-D space, but it also shows something else in yellow that helps the polypeptide keep its correct conformation. These yellow lines are:
- A.
Globular proteins
- B.
Antibodies
- C.
Coils
- D.
Disulfide bridges
- 19.Which level of protein structure would describe a protein or polypeptide as having a-helices or b-pleated sheets?
- A.
Primary
- B.
Secondary
- C.
Tertiary
- D.
Quaternary
- 20.Which level of protein structure would tell you whether a protein is made of more than one polypeptide chain?
- A.
Primary
- B.
Secondary
- C.
Tertiary
- D.
Quaternary
- 21.Which level of protein structure takes into account the total 3-D shape of a protein/polypeptide including its hydrophobic interactions which organize all hydrophobic R-group amino acids into the shielded center of the protein/polypeptide.
- A.
Primary
- B.
Secondary
- C.
Tertiary
- D.
Quaternary
- 22.Which level of protein structure takes into account only the protein's simple sequence of amino acids?
- A.
Primary
- B.
Secondary
- C.
Tertiary
- D.
Quaternary
- 23.How many amino acid changes are required to truly alter the function of a protein? (See the sickle-cell example on p.84)
- A.
1
- B.
2
- C.
3
- D.
More than 10
- 24.If a protein is denatured by heat or chemicals it can actually recover and go back to its functional shape once the heat or chemicals are removed.
- A.
True
- B.
False
- 25.Special proteins that help newly made polypeptides to fold into their 3-D shapes correctly are called ____________________.
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