Ch 3 Proteins – Guided Questions

1. Describe how the structure of an amino acid affects its function and how amino acids
polymerize to form polypeptides.

Amino acids have amine groups, r groups, and carboxyl groups. All three of these groups interact
with one another in folding and in the various forms of structures to serve various functions.

When a peptide bond forms between the amine group’s N and the carboxyl group’s C, H2O is
released. This is the polymerization known as dehydration synthesis. If H2O is added to peptides,
then they both break apart to make individual amino acids. This is known as hydrolysis.

Many peptides coming together make oligopeptides (if they are less than 50) and polypeptides if
they are more than 50. Proteins are functional at the their tertiary structure.

2. On Fig 3.2 from your text book. Explain why R-groups highlighted in green are nonpolar while
those in pink are polar.

R groups in green are nonpolar because they do not have any electronegativity differences/unequal
sharing of electrons. So they are nonpolar and usually hydrophobic. Also, they usually have C and H
because there isn’t much of an electronegativity difference.

R groups in pink are polar because they have a very electronegative element on them. There is an
unequal pull of electrons. Polar groups are usually hydrophilic (like dissolves like). Mostly, they have
oxygen atoms.

3. Order the following amino acids from most hydrophilic to most hydrophobic: valine, aspartate,
asparagine, and tyrosine. Explain.

Aspartate—has a negative O so it is highly polar.

Asparagnine—has both a HO and O so it is somewhat polar.

Tyrosine—has a HO which is less polar.

Valine—doesn’t have any polar elements so it is nonpolar and hydrophobic.

4. Draw the structure of glycine dipeptide.

5. What two functional groups are bound to the central carbon of every free amino acid?

Both the amine group (NH2) and carboxyl group (COOH).

6. Describe the four levels of protein structure and learn the names of the bonds that stabilize
each level of protein structure.

Primary structure: peptide bonds between amino acids

Secondary structure: hydrogen bonds between oxygens and hydrogens (alpha helices or beta
sheets).
Tertiary structure: this is when proteins are functional—caused by the 3D shape when R groups
interact with one another. There are five possibilities:

1) Ionic bonds
2) Covalent bonds
3) Van der waals
4) Hydrogen bonds
5) Hydrophobic interactions

Quaternary structure: not all proteins reach this—this is the interaction between many polypeptides
together.

7. Describe the various roles of proteins in living systems.

The seven roles of proteins include:

- Catalysis
- Defense
- Movement
- Support
- Transport
- Signals