Worksheet 1

Short Response
1. Why is gly a highly conserved a.a.? Your explanation should reference the
Ramachandran plot.
Because glycine has a larger range of conformations that cannot be achieved by
other a.a.s. This is shown via Ramachandran plots; most a.a.s are restricted to the
red region and some go into the yellow region, but glycine has conformations
beyond those colors and can present itself in every quadrant.

:
Glycine can achieve:

further demonstrating its flexible conformations.

2. Name the a.a.
a. All HB
Ala, Gly, Phe, Val, Leu, Met, Ile, Pro, Trp
b. All Hydrophilic (neutral and polar)
Ser, Thr, Cys, Tyr, Asn, Gln
c. All Positively charged
His, Arg, Lys
d. All Negatively Charged
Asp, Glu
e. All Aromatic

Trp, Tyr, Phe

3. What is the purpose of a disulfide bond? Which a.a.(s) take part in this bond?
To stabilize the 3D structure of a protein. Cysteines.
4. Peptide bonds are formed via what reaction.
Dehydrations or condensation reaction
5. Draw Asp-Phe. Label the phi & psi bonds, peptide bond, and the N/C-terminus

6. Beta sheets are composed of what type of strands?

Beta sheets can be composed of all parallel, all anti-parallel, or a mixture of both
beta strands.
7. Proline and Glycine are known as alpha helix breakers, and are typically found
it Beta turns.
8. Coiled coil helices have a heptad repeat pattern in every 8 a.a. to
(increase/decrease) stability.
Multiple Choice
9. Alpha Helices are an example of a proteins:
a. Primary Structure
b. Secondary Structure
c. Tertiary Structure
d. Quaternary Structure
10.Protein Folding is
a. Automatic, mediated by the protein itself
b. Mediated by other proteins called chaperones
c. Mediated by ribosomes
d. None of the above
11.The four subunits of hemoglobin have a
a. Primary and Secondary structure
b. Tertiary structure
c. All of the above

d. Quaternary structure
12.Which of the following is an example of a tertiary structure
a. A multimeric protein
b. An alpha helix
c. A beat pleated sheet
d. A globular domain
13.The portion of proteins having the highest mobility are
a. Alpha helices
b. Beta sheets
c. Peptide bonds
d. Surface side chains
e. Aliphatic groups
14.Which of the following is most correct
a. Charged amino acids are never buried inside a protein
b. Glycine is rarely found in proteins because it is too destabilizing
c. Phenylalanine is only found in the interior of a protein
d. Charged amino acids are seldom buried inside a protein
15.Disulfide bonds mostly stabilize the native structure of
a. Extracellular proteins
b. Dimeric proteins
c. HB proteins
d. Intracellular proteins
e. Multi-subunit proteins
16.An alpha helix does NOT have
a. 3.66 residues per 100 degree turn
b. 5.4 Angstroms per turn
c. Polar side chains typically face outside the coiled structure
d. Non polar side chains typically face inside
Identify the Motif

Beta barrel
(up/down beta
sheet)

Helix-turnhelix

Globin Fold

Beta barrel (greek key)

Helical bundle

Beta
propellers

Beta-alpha-beta

Open twisted sheet

(alpha/beta)