Name: Shannon Kelso

Access ID: smk5736

Week 4 - Exploration Homework: Transcription and Translation
Part I - Splicing
Last week we started into the topic of transcription and well finish up this week and then move
onto translation. Heres a nice animation from McGraw-Hill giving a general overview of RNA
splicing. For a more in-depth look, heres another from NDSU that includes many of the
structures we will discuss in class. Read the Wikipedia article Splicesome (Intro and
Composition).
1. What is the major role of the splicesome?
To remove introns from pre-mRNA thats already been transcribed.
2. What are the two major molecules in a spliceosome?
snRNAs & protein complexes
3. What are snRNA? What is snRNP? How are these two molecules related?
snRNA is small, nuclear ribonucleic acid, & snRNP are small, nuclear ribonucleic
proteins. snRNAs form together with protein to create snRNP.
4. In terms of post-transcriptional processing, whats so important about the nucleotides GU
and AG within an intron?
At the 5 end is the GU nucleotide, & at the 3 end is the AG nucleotide. U1 binds to the 5
end to splice the intron.
Part II - Protein Translation
Use the Wikipedia articles tRNA (Intro section) and Translation (biology) (Intro Section). The
Virtual Cell Animation Collection website has several good animations for the overview of
translation, while this second animation from the DNA Learning Center provides a more realistic
view of the process.
5. One end of a tRNA contains _____________ while the other contains ________________.
The anticodon while the other contains the covalent attachment for the anticodon
sequence.
6. What is the function of aminoacyl-tRNA synthetase?
To activate the amino acid by using ATP hydrolysis energy so that it forms the
aminoacyl-AMP.
7. What are the four major stages of translation?
Initiation, Elongation, Translocation, & Termination.
8. The first codon on virtually all mRNAs is _____.
The start codon. Its usually AUG & in eukaryotes the start codon codes for methionine.

Part III - Protein Translation (Rough Endoplasmic Reticulum)

Use the Wikipedia article Endoplasmic reticulum (Structure: Rough Endoplasmic Reticulum) to
answer the following questions.
9. Ribosomes present in the RER are stable and associate with the RER over a long period of
time. True or False.
False, the ribosomes are not stable because they are being bound & released to the ER
regularly.
10. Under what conditions will a ribosome associate with the RER?
A ribosome will bind the RER whenever proteins are ready to be synthesized.
11. What types of molecules make up the translocon?
Protein complexes make up the translocon.
12. What two major functions does the translocon complete?
It translocates polypeptides across the membrane, & it can also translocate/integrate
membrane proteins into the ER.

Part IIII Protein Structure

Use the Wikipedia article Protein Structure - Intro to answer the following questions.
13. What interactions contribute to the overall shape (folding) of a protein?
Hydrogen bonding, ionic interactions, Van der Waals forces, & hydrophobic packing.
14. What makes up the primary structure of a protein? What bonds contribute to this structure?
Proteins are polypeptides that are made up of amino acid monomers. Theyre held by
covalent bonds or peptide bonds.
15. What are the two main types of secondary structure? What bonds contribute to this
structure?
The alpha helix & beta strand. They are formed by hydrogen bonds between the peptide
chains.
16. What forces are involved with formation of protein tertiary structure?
Non-specific hydrophobic interactions, & is stabilized with salt bridges, and hydrogen
bonding.
17. What is quaternary structure of a protein?
A 3D structure of a multi-subunit protein.
18. What is the definition of a protein structural domain? Why are they important?
A self-stabilizing element that usually will fold separately from the rest of the protein.
These can be swapped with another protein to create chimera proteins.