All GRE Subject Test: Biochemistry, Cell, and Molecular Biology Resources
Example Questions
Example Question #31 : Rna, Transcription, And Translation
In prokaryotes what site on the mRNA does the ribosome bind to initiate translation?
The operator
The poly adenine tail
The Shine-Dalgarno sequence
The promoter
The 3' untranslated region
The Shine-Dalgarno sequence
The Shine-Dalgarno sequence is the ribosomal binding site in in prokaryotic mRNA that is located around 8 bases upstream of the start codon.
Example Question #471 : Gre Subject Test: Biochemistry, Cell, And Molecular Biology
Which of the level of protein structure is incorrectly matched to its description?
Secondary structure is determined by hydrogen bonding of the amino acid backbone
Primary structure is the linear amino acid sequence of a protein
Quaternary structure is the three-dimensional structure of a multi-subunit protein
Tertiary structure is the two-dimensional structure of a protein
Tertiary structure is the two-dimensional structure of a protein
Primary structure of a protein is determined by covalent peptide bonds, and corresponds to the linear sequence of amino acids before structures begin to form. Secondary structure results from hydrogen bonding between the amino acid backbones to form alpha-helices and beta-sheets. Tertiary structure is formed when functional groups of the amino acids interact, either by hydrogen bonding, hydrophobic interactions, or disulfide bridge formation. Tertiary structure is associated with the three-dimensional structure of a single polypeptide chain. Quaternary structure forms when multiple polypeptide chains interact to build a multi-subunit structure.
Example Question #32 : Rna, Transcription, And Translation
Which of the following proteins are likely to contain leucine zipper domains?
Transcription factors
Transmembrane proteins
Lipases
Proteases
Transcription factors
Leucine zippers are domains that allow for the binding of DNA. The question is essentially asking, "which of these proteins are capable of binding DNA?"
Proteases cleave proteins, lipases hydrolyze lipids, and transmembrane proteins interact with membranes. Transcription factors are the only given proteins that bind DNA and, therefore, are much more likely to contain leucine zipper domains than the other options.
Example Question #1 : Help With Protein Structures
Which protein structure involves the binding of multiple polypeptides?
Primary structure
Tertiary structure
Quaternary structure
Secondary structure
Quaternary structure
The structures of a protein increase in complexity all the way up to quaternary structure. Primary structure is based on the amino acid sequence of the protein, while secondary and tertiary structures are based on intermolecular attractions between the amino acids in the polypeptide. Quaternary structure is only seen when a functional protein complex is composed of two or more polypeptides bound together.
Example Question #42 : Rna, Transcription, And Translation
Disulfide bonds in proteins are categorized under which structure class?
More than one of these
Quaternary structure
Tertiary structure
Primary structure
Secondary structure
More than one of these
The correct answer is more than one of these. Primary structure is defined as a succession of amino acids joined by peptide bonds. Secondary structure introduces dimensionality to a protein via hydrogen bonding to produce two predominant structures, alpha helices and beta-pleated sheets. Tertiary structures cause further protein folding by disulfide bonds between cysteines, Van der Waal interactions, and hydrophobic interactions. Quaternary structures involve multiple amino acid chains folding together, and utilize the same types of bonds as tertiary structures.
Example Question #43 : Rna, Transcription, And Translation
The 5' cap on eukaryotic mRNA molecules is recognized by which of the following proteins?
RNA polymerase
PABP
eIF4e
40s ribosomal subunit
eIF4e
The 5' cap is recognized by the important translation factor eIF4e. Once bound, eIF4e helps transport the mRNA molecule to the ribosome and facilitates bonding to the ribosomal machinery.
The 3' poly-A tail is recognized by PABP. RNA polymerase is involved in transcription, not translation. The 40s ribosomal subunit is recruited by the initiation complex (including eIF4e, PABP, and various other translation factors).
Example Question #11 : Translation And Proteins
When conducting a stain of chromosomes, certain regions along the chromosome will stain more darkly than the rest. This is due to the fact that these regions are more tightly condensed. What is the functional outcome of having one region more condensed (heterochromatin) than the rest (euchromatin)?
Heterochromatin is typically not transcribed/transcribed at a lower rate because the tight packing limits accessibility to polymerases.
Heterochromatin does not contain any genes and is a structural component of the chromosome.
Heterochromatin is not transcribed/is transcribed at a lower rate because euchromatin saturates all available polymerase.
Heterochromatin is transcribed at a high frequency because there are a high number of genes in a small area.
Heterochromatin unpacking requires many ATP and is energetically expensive.
Heterochromatin is typically not transcribed/transcribed at a lower rate because the tight packing limits accessibility to polymerases.
Heterochromatin often contains simple, repetitive sequences, and although it cannot be said that it is completely void of coding sequences, it is not typically transcribed. The tight wrapping prevents polymerase from accessing the strand, and euchromatin typically contains the regions that get transcribed. Thus, heterochromatin is though to contain repressed or inactive genes.
Example Question #45 : Rna, Transcription, And Translation
Small GTPases are important molecular switches and signaling pathways. What proteins are responsible for promoting the activation of these small GTPases?
Kinases
Nicotinamide adenine dinucleotide
Guanine triphosphate
Phosphatases
Guanine nucleotide exchange factors
Guanine nucleotide exchange factors
The correct answer is guanine nucleotide exchange factors. In order to activate small GTPases and subsequently stimulate downstream pathways, guanine nucleotide exchange factors bind inactive GTPases and cause the release of guanine diphosphate (GDP). This allows guanine triphosphate (GTP) to bind and active the GTPase.
Example Question #46 : Rna, Transcription, And Translation
Which of the following is not an example of post-translational modification?
Ubiquitination
Alkylation
Polyadenylation
Myristoylation
Polyadenylation
Polyadenylation is an example of post-transcriptional modification. This process involves adding large repeats of adenine bases to the 3' end of mRNA molecules, known as the poly-A tail.
Myristoylation is the process of adding myristate (a fatty acid) to a protein, alkylation is the process of adding an alkyl group, and ubiquination is the process of adding a molecule of ubiquitin (a small protein often used to signal degradation).
Example Question #47 : Rna, Transcription, And Translation
In which of the following organelles does the initial linkage of a sugar for post-translation modification N-linked glycosylation most commonly occur?
Mitochondria
Nucleus
Golgi apparatus
Endoplasmic reticulum
Endoplasmic reticulum
Two of the more common types of glycosylation, N-linked and O-linked, occur at different points and in different places in the cell. N-linked glycosylation takes place in the lumen of the endoplasmic reticulum, while O-linked glycosylation takes place in the Golgi body.
The other options, the mitochondria and the nucleus, are not involved in these post-translational modifications.