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Topic 7.3 Review Practice Questions

The document contains review practice questions about translation. It defines the key sites on a tRNA molecule including the acceptor stem, t arm, anticodon, and D arm. There are 20 types of tRNA and associated charging enzymes in a cell. The charging process involves a tRNA activating enzyme binding ATP and an amino acid to form a complex with a specific tRNA, attaching the amino acid. Ribosomes have a small subunit that initiates translation and a large subunit that catalyzes peptide bond formation. Eukaryotic ribosomes are larger and associated with the ER, while prokaryotic ribosomes are smaller and in the cytoplasm. A polysome is a cluster of ribosomes making multiple copies of a

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0% found this document useful (0 votes)
78 views5 pages

Topic 7.3 Review Practice Questions

The document contains review practice questions about translation. It defines the key sites on a tRNA molecule including the acceptor stem, t arm, anticodon, and D arm. There are 20 types of tRNA and associated charging enzymes in a cell. The charging process involves a tRNA activating enzyme binding ATP and an amino acid to form a complex with a specific tRNA, attaching the amino acid. Ribosomes have a small subunit that initiates translation and a large subunit that catalyzes peptide bond formation. Eukaryotic ribosomes are larger and associated with the ER, while prokaryotic ribosomes are smaller and in the cytoplasm. A polysome is a cluster of ribosomes making multiple copies of a

Uploaded by

Glen Joji
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Topic 7.

3 Review Practice Questions

1) Identify the sites on the tRNA molecule, and include the function of
each

1) acceptor stem - carries a amino acid

2) t arm - contains mRNA codon

3) anticodon - contains the ribosome

4) D arm - contains tRNA activating enzym

Key region information can be found here:


https://ib.bioninja.com.au/higher-level/topic-7-nucleic-acids/73-translation/ribosomes-
and-trna.html

2) Summarize the process in which tRNAs are “charged” with their respective amino
acids. Be sure to include how many types of tRNA and charging enzymes are present in
a cell.

1) tRNA - activating enzyme


2) Enzyme binds to ATP and a specific amino acid
3) amino acid - AMP complex is formed and a specific tRNA molecule is recruited
4) The tRNA is bound to the amino acid and AMP is released
5) “Charged” tRNA is produced

3) Outline the two major structures of a ribosome and list the functions of each.

Small Ribosomal Subunit:


Function: Initiates protein synthesis by binding to mRNA and positioning the initiator
tRNA for translation.

Large Ribosomal Subunit:

Function: Catalyzes peptide bond formation between amino acids during protein
synthesis and contains tRNA binding sites and an exit tunnel for the growing polypeptide
chain.

4) Differentiate between the following ribosomes:

A) Eukaryotic vs. Prokaryotic Ribosomes:

Size:

Eukaryotic: Eukaryotic ribosomes are larger and consist of a small (40S) and a large (60S)
subunit, totaling 80S in size.
Prokaryotic: Prokaryotic ribosomes are smaller and consist of a small (30S) and a large (50S)
subunit, totaling 70S in size.

Location:

Eukaryotic: Eukaryotic ribosomes are found in the cytoplasm and can also be associated with
the endoplasmic reticulum (ER) when synthesizing proteins for export or membrane
incorporation.
Prokaryotic: Prokaryotic ribosomes are primarily found in the cytoplasm, as prokaryotic cells
lack membrane-bound organelles like the ER.

B) Fixed E.R. Ribosomes vs. Free Cytoplasmic Ribosomes:

Location:

Fixed E.R. Ribosomes: These ribosomes are attached to the endoplasmic reticulum (ER)
membrane. They are involved in synthesizing proteins that are either secreted from the cell,
inserted into membranes, or sent to specific organelles.

Free Cytoplasmic Ribosomes: These ribosomes float freely in the cytoplasm. They synthesize
proteins that remain in the cytoplasm or are targeted to organelles like the mitochondria or
nucleus.
Function:
Fixed E.R. Ribosomes: They synthesize proteins destined for export from the cell, incorporation
into cell membranes, or entry into specific organelles. These proteins typically have a signal
sequence that directs them to the ER.

Free Cytoplasmic Ribosomes: They synthesize proteins primarily used within the cytoplasm.
These include enzymes, structural proteins, and proteins involved in various cellular processes.

5) Use the diagram below to explain the three stages of translation:

A) Initiation- The start of protein synthesis when the ribosome assembles on mRNA and
begins reading the genetic code.

B) Elongation- The middle stage of protein synthesis where amino acids are added one
by one to the growing protein chain.

C) Termination- The end of protein synthesis when the ribosome releases the completed
protein from the mRNA.
6) Define a Polysome, and determine how a researcher could distinguish between a
prokaryotic and eukaryotic version of a microscopic image of it.

A polysome is a cluster of ribosomes working together to make multiple copies of a


protein from a single set of instructions (mRNA) in a cell.

Prokaryotic: In prokaryotic cells, which are simpler and lack a nucleus, polysomes are
scattered throughout the cell's cytoplasm.

Eukaryotic: In eukaryotic cells, which are more complex and have a nucleus, polysomes
can be found on the endoplasmic reticulum (ER) or freely dispersed in the cytoplasm.
Look for membrane structures and consider cell size in the image to distinguish between
them.

7) Summarize the four stages of a protein’s structure using the diagram below:

Primary: sequence of amino acids, uses peptide bonds

Secondary: local folding or turning to form either an A helix or a B helix, hydrogen


bonding within the amine and carboxyl groups

Tertiary: continued folding of the protein into a 3D shape, interactive bonds within the
functional groups within the protein, and hydrogen, disulfide bonds, ionic bonding, van
der waals forces.
Quaternary: interaction of multiple protein tertiary structures, same as tertiary within the
interacting subunit of each part of the multimer.

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