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Example Questions
Example Question #31 : Dna, Rna, And Proteins
The genetic code is composed of only four nucleotides. Each codon that is read by a ribosome is composed of a distinct three-nucleotide sequence.
There are sixty-four total codons that can be made using four different nucleotides, however, there are only twenty different amino acids created by ribosomes. What is the reason for this discrepancy?
Each codon will code for only one amino acid.
Some combinations of nucleotides are not observed in nature.
More than one codon sequence can code for the same amino acid.
Ribosomes are unable to "read" certain codons, and will not translate the mRNA as a result.
More than one codon sequence can code for the same amino acid.
The genetic code is described as degenerative, meaning that more than one codon may code for the same amino acid.
While it is true that a codon will only code for one amino acid, this does not explain why there is a difference in the number of possible codons and amino acids. All combinations of three nucleotides are observed in nature, and ribosomes are capable of reading all possible codons.
Example Question #1 : Translation
A mutation causes the insertion of a single nucleotide into a template strand of DNA. How will the mutant protein compare to the wild type protein?
The mutant protein will differ from the original protein by one amino acid.
Both of the proteins will be the same. No change will be witnessed.
The mutant protein will be completely different from the original protein, differing in both length and amino acid sequence.
The ribosome will only translate the original mRNA strand. It will stop translating the mutant strand once it reaches the mutation.
The mutant protein will be completely different from the original protein, differing in both length and amino acid sequence.
The insertion or deletion of one base pair to a strand of mRNA results in a frameshift mutation. Because ribosomes read mRNA by reading three nucleotides at a time, the addition of another nucleotide can completely alter the reading frame, thus the name of the mutation. The ribosome will now be reading completely different codons, and the mutant protein will look entirely different from the original protein. The shift will also affect the "stop" codon, likely leading to early termination and a shorter protein.
The alteration of only one amino acid is typically seen when one nucleotide is replaced by another nucleotide, so this would not be seen in this case.
Example Question #4 : Translation
Most scientists subscribe to the theory of endosymbiosis to explain the presence of mitochondria in eukaryotic cells. According to the theory of endosymbiosis, early pre-eukaryotic cells phagocytosed free living prokaryotes, but failed to digest them. As a result, these prokaryotes remained in residence in the pre-eukaryotes, and continued to generate energy. The host cells were able to use this energy to gain a selective advantage over their competitors, and eventually the energy-producing prokaryotes became mitochondria.
In many ways, mitochondria are different from other cellular organelles, and these differences puzzled scientists for many years. The theory of endosymbiosis concisely explains a number of these observations about mitochondria. Perhaps most of all, the theory explains why aerobic metabolism is entirely limited to this one organelle, while other kinds of metabolism are more distributed in the cellular cytosol.
Scientists studying endosymbiosis often support the theory by referencing the differences between mitochondria and other membrane-bound organelles, as the passage discusses. Which of the following is NOT a membrane-bound organelle?
Ribosomes
Golgi apparatus
Endosome
Nuclei
Rough endoplasmic reticulum
Ribosomes
Ribosomes are the only answer choices not bound by a membrane. Prokaryotes do not have membrane bounded organelles, but do have ribosomes to translate their RNA into proteins.
Example Question #143 : Cell Biology, Molecular Biology, And Genetics
In 2013, scientists linked a cellular response called the unfolded protein response (UPR) to a series of neurodegenerative diseases, including such major health issues as Parkinson’s and Alzheimer’s Disease. According to their work, the unfolded protein response is a reduction in translation as a result of a series of enzymes that modify a translation initiation factor, eIF2, as below:
In the above sequence, the unfolded protein sensor binds to unfolded protein, such as the pathogenic amyloid-beta found in the brains of Alzheimer’s Disease patients. This sensor then phosphorylates PERK, or protein kinase RNA-like endoplasmic reticulum kinase. This leads to downstream effects on eIF2, inhibition of which represses translation. It is thought that symptoms of neurodegenerative disease may be a result of this reduced translation.
Which of the following is true of the ribosomes central to translation, as discussed in the passage?
Ribosomes bind to tRNA first, followed by mRNA binding
Ribosomes are only found in eukaryotes
Each ribosome can harbor up to five tRNA molecules at a time
Ribosomes are the site of extensive protein modification conicident with translation
The rRNA that makes up ribosomes is transmitted from the nucleolus, through nuclear pores, to the cytosol
The rRNA that makes up ribosomes is transmitted from the nucleolus, through nuclear pores, to the cytosol
Ribosomes are the main place where rRNA is used in cells. The rRNA makes up a portion of the ribosome structure, and this rRNA is made in the nucleolus before leaving the nucleus via nuclear pores
The remaining choices are all false. Ribosomes are found in both prokaryotes and eukaryotes and can hold two tRNA molecules (though they have three binding sites). Ribosomes bind to mRNA during translation, but most protein modification occurs later in the endoplasmic reticulum.
Example Question #6 : Translation
In 2013, scientists linked a cellular response called the unfolded protein response (UPR) to a series of neurodegenerative diseases, including such major health issues as Parkinson’s and Alzheimer’s Disease. According to their work, the unfolded protein response is a reduction in translation as a result of a series of enzymes that modify a translation initiation factor, eIF2, as below:
In the above sequence, the unfolded protein sensor binds to unfolded protein, such as the pathogenic amyloid-beta found in the brains of Alzheimer’s Disease patients. This sensor then phosphorylates PERK, or protein kinase RNA-like endoplasmic reticulum kinase. This leads to downstream effects on eIF2, inhibition of which represses translation. It is thought that symptoms of neurodegenerative disease may be a result of this reduced translation.
In which type of cell would a factor such as eIF2 be most active?
Necrotic cell
Secretory cell
Keratinocyte
Sperm cell
Apoptotic cell
Secretory cell
We know that inhibition fo eIF2 represses traslation. The question asks for the cells where eIF2 is most active, thus where translation is likely at its higest.
Secretory cells make protein secretions, such as Goblet cells or pancreatic acinar cells. These protein secretions are the product of translation, which requires eIF2 to function, based on the passage.
Keratinocytes form the outermost layer of the dermis, sperm cells are essential to reproduction, and apoptotic and necrotic cells are in the process of cell death; none of these will put significant energy into the translation of proteins.
Example Question #151 : Cell Biology, Molecular Biology, And Genetics
In the crusade to create a vaccine for Poliomyelitis, Jonas Salk and Albert Sabin created two separate vaccines that proved to be successful in preventing Polio onset.
The Salk vaccine, which is given by standard injection, contained virus particles inactivated by an organic solvent. This method has the advantage of inactivating each of the three Polio strains with no bias.
Albert Sabin's vaccine, given by oral inoculation via sugar water, contained live virus particles that had been genetically attenuated. With this method, each of the three Polio strains acquired separate mutations that made them unable to infect the human host cells. Strain 2 in particular contained one single nucleotide polymorphism in the internal ribosomal entry site (IRES) that prevented successful viral replication.
What is the function of the internal ribosomal entry site (IRES) utilized by the Poliovirus?
The IRES provides an alternate site of entry that allows loading of viral mRNA onto the ribosome for translation
The IRES is encoded by the host and prevents loading of viral mRNA onto the ribosome
The IRES allows the viral ribosome to out-compete the host ribosome, thus allowing for greater translation of viral proteins
The IRES facilitates interaction between the large and small ribosomal subunits, which contributes to viral mRNA translation
The IRES provides an alternate site of entry that allows loading of viral mRNA onto the ribosome for translation
Poliovirus mRNA is not capped, and therefore cannot be loaded onto host ribosomes for translation. To overcome this, viral mRNA contains an internal ribosomal entry site (IRES) sequence that allows it to bind and bring the translational machinery in close contact with the start codon to initiate translation.
Example Question #1191 : Biology
Which of the following statements about translation is incorrect?
The mRNA first attaches to the small ribosomal subunit
The mRNA is "read" by the ribosome in a 5' to 3' direction
The tRNAs that have given up their amino acid can exit the ribosome at the E site
New tRNAs with an amino acid enter the ribosomal complex at the P site
New tRNAs with an amino acid enter the ribosomal complex at the P site
Make sure that you know the three steps of translation: initiation, elongation, and termination. The order of the three sites available to a tRNA in the ribosome are A, P, and E. New tRNAs with an amino acid attached enter the ribosome at the A site. The tRNA that previously occupied the A site is pushed to the P site, with the growing polypeptide attached to it. It then gives the polypeptide to the next tRNA in the A site, and the now amino acid deficient tRNA can exit at the E site.
All other answer choices are true.
Example Question #1191 : Biology
Type 1 diabetes is a well-understood autoimmune disease. Autoimmune diseases result from an immune system-mediated attack on one’s own body tissues. In normal development, an organ called the thymus introduces immune cells to the body’s normal proteins. This process is called negative selection, as those immune cells that recognize normal proteins are deleted. If cells evade this process, those that recognize normal proteins enter into circulation, where they can attack body tissues. The thymus is also important for activating T-cells that recognize foreign proteins.
As the figure below shows, immune cells typically originate in the bone marrow. Some immune cells, called T-cells, then go to the thymus for negative selection. Those that survive negative selection, enter into general circulation to fight infection. Other cells, called B-cells, directly enter general circulation from the bone marrow. It is a breakdown in this carefully orchestrated process that leads to autoimmune disease, such as type 1 diabetes.
When activated, T-cells use a number of proteins to kill cells that they recognize as foreign. A scientist develops an experimental drug to treat autoimmune disease by disrupting one of these proteins. The drug degrades the cytosolic mRNA for this protein in a T-cell. Which of the following is true if this drug is used successfully?
I. The protein is synthesized, but in an inactive form
II. The protein gene is transcribed
III. The total complement tRNA used for synthesis of the protein is not mobilized to active ribosomes
II, only
I and III
I, II, and III
II and III
III, only
II and III
The successful use of the drug implies that the mRNA is degraded before it can be used in translation. As a result, the tRNAs used for the translation would not be mobilized for use on translating ribosomes, but transcription of mRNA would be unimpeded. The protein gene would be transcribed, the mRNA would be modified and leaves the nucleus, and would then be degraded before any synthesis could occur.
Example Question #1192 : Biology
Temperature sensitive (Ts) mutations are a powerful genetic tool in yeast and fruit flies. Ts mutations allow researchers to examine biological functions of specific genes at permissive (phenotypically normal) and restrictive (phenotypically abnormal) temperatures. What is the likely result of the Ts mutation at the restrictive temperature?
Biological processes, such as transcription and translation, are globally impaired
The gene that is mutated is only required at the restrictive temperature
The protein arising from the mutated gene does not fold properly
Cells undergo apoptosis
The protein arising from the mutated gene does not fold properly
The temperature sensitive (Ts) mutation to a given gene results in a less stable protein product. At higher temperatures the protein does not fold properly or "melts," resulting in an improper structure of the protein. In turn, this improper structure will inhibit its function.
The Ts mutation will only affect a single gene, and is unlikely to affect global functions or cause apoptosis. Very few genes are only required at specific temperatures (genes required for stress response is an example). It is possible that the gene in question is required only at the restricted temperature, however, this is not the likely cause.
Example Question #12 : Translation
In 2013, scientists linked a cellular response called the unfolded protein response (UPR) to a series of neurodegenerative diseases, including such major health issues as Parkinson’s and Alzheimer’s Disease. According to their work, the unfolded protein response is a reduction in translation as a result of a series of enzymes that modify a translation initiation factor, eIF2, as below:
In the above sequence, the unfolded protein sensor binds to unfolded protein, such as the pathogenic amyloid-beta found in the brains of Alzheimer’s Disease patients. This sensor then phosphorylates PERK, or protein kinase RNA-like endoplasmic reticulum kinase. This leads to downstream effects on eIF2, inhibition of which represses translation. It is thought that symptoms of neurodegenerative disease may be a result of this reduced translation.
Which of the following is true of the process of translation discussed in the passage?
Translation converts rRNA into protein
rRNA is an important component of the translation machinery
Translation relies on anticodons in mRNA to bind to codons on tRNA
Translation relies on membrane-bound ribosomes
Translation takes place in the nucleus
rRNA is an important component of the translation machinery
rRNA is an important building block of ribosomes, which synthesize proteins.
The anticodons of tRNA (not mRNA) bind to codons of mRNA (not rRNA), allowing ribosomes to tie together amino acids shuttled in on tRNA molecules. Many ribosomes are bound to the rough endoplasmic reticulum, but are not commonly bound to the membrane of the cell.
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