3.Decide on one plan and assign responsibilities to
each member of your group.
4.Assemble the materials you will need and prepare
your presentation.
Checking the Plan
1.Check your plan against your initial list of the
structures, molecules, and processes involved
in protein synthesis. Have you included all the
important steps?
2.Do the materials you are using help to explain the
processes involved at each step?
3.Has your teacher approved your plan?
Data and Observations
Present your simulation of protein synthesis to the class.
Make a note of any comments you receive from other
groups. Identify which parts of your presentation seemed
to be the most effective at simulating protein synthesis.
Do these results match your initial hypothesis?
Analyze
1.Among the different approaches used by the groups
in the class, which do you think was the most
effective? Explain.
2.Now that you have seen how other groups
approached the problem, how would you revise
your own presentation?
Conclude and Apply
3.Identify three ways in which the two-step process of
protein synthesis helps living cells conserve energy
or reduce the risk of damage from mutations.
4.What are the adaptive advantages and disadvantages
of the presence of introns in eukaryotic cells?
Exploring Further
5.Almost all living organisms on Earth use the same
20 amino acids. However, molecular biologists have
been able to develop a number of artificial amino
acids, which can be used to develop synthetic
proteins that have many potential applications. In
response, some research teams are exploring the
possibility of expanding the genetic code to include
new nucleotides that could be used to code for
artificial amino acids. Use your library or the Internet
to find out more about this research. Write a brief
report explaining some of the hurdles that will have
to be overcome as scientists try to expand the
genetic code. What are some of the scientific and
social implications of this research?
Chapter 8 Protein Synthesis • MHR 267
mRNA
5 ′ 3 ′
E
E
E
P
P
A
A
PA
growing polypeptide incoming
aa-tRNA
molecule
new peptide
bond being
transferred
ribosome
ready for
next aa-tRNA
molecule
Figure 8.19The three steps of the elongation cycle. Once initiated, this cycle will
continue until the protein synthesis equipment encounters a stop signal.
The anticodon of an aa-tRNA
molecule binds to the mRNA
codon exposed in the A site.
A
Enzymes and other
molecules in the
ribosome catalyze the
formation of a bond
between the last
amino acid on
the lengthening
polypeptide and
the new amino acid.
B
The ribosome moves down
the mRNA strand, shifting the
binding sites a distance of
three nucleotides. A new A site
is exposed as the tRNA that
was in the P site is moved to
the E site and released.