Cells and Cell parts
Transcription
Translation
Protein folding
Protein function
100

Process whereby genes were moved from an ancestral bacteria to eukaryotic nucleus resulting in the mitochondria and chloroplast not able to leave the host cell.

What is horizontal gene transfer?

100

Transcription factor that opens double helix and adds phosphates to CTD (Ser) domain of RNA pol II.

What is TFIIH?

100

Factor that brings in initatior tRNA with Met.

What is eIF2?

100

Oh no! a new polypeptide is coming out of the exit tunnel of the ribosome but has a stretch of hydrophobic amino acids and is folding incorrectly. What protein can help?

What is Hsp 70?

100

Proteins with ubiquitin added to Lys48 will go here.

What is the proteasome?

200

Organelle that detoxifies with catalase and also aids break down of fats.

What is the peroxisome?

200

RNA + protein complexes involved in intron removal in the nucleus of eukaryotic cells. 

What are snRPs/ What is the spliceosome?

200

Ribozyme that facilitates peptide bond formation from growing polypeptide on tRNA in P site to amino acid on tRNA in A site.

What is 28s rRNA or peptidyl transferase?

200

Nothing helps. No matter how many times Hsp 60 tries, a protein won't fold correctly. What is it tagged with and where does it go?

What is ubiquitin and what is the proteosome?

200

A mutation has occurred in EF2 resulting in a higher Km than usual. What does this mean for ribosome translocation?

What is loose binding resulting in poor translocation?

300

Just because an organism has more DNA, does not mean that organisms is more complex. 

What is the C-value paradox?

300

CstF and CPSF

What are cutting factors that bind to the poly A signal (AAUAAA) and facilitate cutting of transcript for addition of poly A tail?

300

Ability to check for incoming tRNA anticodon to codon match requires the 18s rRNA to bind tightly causes this to hydrolyze and release a phosphate so that EF1 will let go of the tRNA to settle in the A site of the ribosome. 

What is GTP?

300

Protein structure formed from hydrogen bonds between amino heads and carboxyl tails of the amino acid back bone. 

What is secondary structure? What are beta-pleated sheets, alpha helices, and coiled-coils?

300

For a given enzyme, 20 substrate molecules are converted to product/ sec with a turnover rate of 5 substrates converted to product/ sec/ molecule of enzyme. How many molecules of enzyme are there in this situation?

What is 4?

400

Cells that contain membrane-bound organelles including a nucleus.

What are eukaryotes?

400

A mutation in the TBP (TATA box binding protein) results in high Km values. (Hint: What would this mean for transcription?)

What is reduced transcription due to poor binding of promoter region.

400

UGA, UAA, UAG

What are the stop codons?

400

The amino acids Proline Valine and Tryptophan line a binding site for a specific protein. What charge would the ligand that fits into this binding site have?

What is hydrophobic?

400

Magnesium and iron are just two examples of molecules important for protein function. 

What are cofactors?

500

Organelle that stores calcium, synthesizes lipids, and completes some protein translation.

What is the endoplasmic reticulum?

500

Three proteins that aid movement of RNA out of nuclear pore complex.

What are nuclear transport receptors, cap binding complex (CBC), poly A binding proteins.

500

Factor that adds a water molecule to the carboxyl terminus of the growing polypeptide chain when a stop codon is reached during translation. 

What is the release factor?

500

Regions (substructure) of a protein that fold independent of other regions and result in specific function.

What is a domain?

500

When one molecule X binds to a site other than the active site of enzyme A (a multi-subunit enzyme) this leads to all subunits of enzyme A opening at the same time.

What is cooperative allosteric transition? or What is positive coupled linkage?

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