a. it will spontaneously proceed. | ||
b. it will always remain at equilibrium. | ||
c. it will only proceed if coupled with a reaction that results in a greater decrease in G. | ||
d. it will only proceed if the resultant increase in G is immediately used by the cell. |
a. Polar molecules | ||
b. Nonpolar molecules | ||
c. Ions | ||
d. Inorganic molecules |
a. Carbohydrates | ||
b. Lipids | ||
c. Inorganic ions | ||
d. Nucleic Acids |
a. Carbohydrates | ||
b. Lipids | ||
c. Proteins | ||
d. Nucleic Acids |
a. Carbohydrates | ||
b. Lipids | ||
c. Proteins | ||
d. Nucleic Acids |
a. Carbohydrates | ||
b. Lipids | ||
c. Proteins | ||
d. Nucleic Acids |
a. Primary | ||
b. Secondary | ||
c. Tertiary | ||
d. Quaternary |
a. Primary | ||
b. Secondary | ||
c. Tertiary | ||
d. Quaternary |
a. Primary | ||
b. Secondary | ||
c. Tertiary | ||
d. Quaternary |
a. A membrane channel | ||
b. A membrane carrier | ||
c. A membrane pump | ||
d. A peripheral protein |
a. Calcium-triggered muscle contraction, particularly in cardiac muscle, would be facilitated. | ||
b. Glucose concentrations outside of cells would decline. | ||
c. Cells would become more acidic. | ||
d. Glucose concentrations inside of cells would decline. |
a. Enzymes that regulate the double bonds in membrane fatty acids would increase the number of double bonds. | ||
b. Enzymes that regulate the chain length of membrane fatty acids would make longer-chain fatty acids. | ||
c. Enzymes that regulate the chain length of membrane fatty acids would make shorter-chain fatty acids. | ||
d. Enzymes that regulate the incorporation of cholesterol in membranes would add more cholesterol to membranes. |
a. Membrane ion channels | ||
b. Membrane lipids | ||
c. Membrane proteins | ||
d. Membrane glycogens |
a. A molecule of glucose is transported into the cell via a membrane carrier. | ||
b. To remove calcium from the cell, the expulsion of one molecule of calcium is coupled with the intake of three molecules of sodium. | ||
c. Epithelial cells in the intestine are able to take up glucose by coupling this reaction with the uptake of two molecules of sodium. | ||
d. To prevent acidification of the cytoplasm, the expulsion of one proton is coupled with the intake of one molecule of sodium. |
a. A molecule of glucose is transported into the cell via a membrane carrier. | ||
b. To remove calcium from the cell, the expulsion of one molecule of calcium is coupled with the intake of three molecules of sodium. | ||
c. Epithelial cells in the intestine are able to take up glucose by coupling this reaction with the uptake of two molecules of sodium. | ||
d. To prevent acidification of the cytoplasm, the expulsion of one proton is coupled with the intake of one molecule of sodium. |
a. In human cell membranes, it makes membranes more rigid (viscous) at higher temperatures but more fluid at lower temperatures. | ||
b. In human cell membranes, it makes the transition from lower to higher viscosity (phase transition) more steep and abrupt. | ||
c. In human cell membranes, it makes membranes more rigid. | ||
d. Cholesterol only functions as a membrane-structuring component in bacterial cells. |
a. Membranes are composed primarily of phospholipids and proteins. | ||
b. Some trans-membrane proteins have many membrane-spanning regions. | ||
c. The lipid and/or protein composition of membranes varies, depending on the type of membrane. | ||
d. The lipid composition of membranes is always 50%. |
a. A ligand-gated ion channel | ||
b. A voltage-gated ion channel | ||
c. A membrane carrier | ||
d. A membrane pump |
a. G-protein-coupled receptors | ||
b. Receptor tyrosine kinases | ||
c. Cytokine receptors | ||
d. Receptor serine/threonine kinases |
a. G-protein-coupled receptors | ||
b. Receptor tyrosine kinases | ||
c. Cytokine receptors | ||
d. Guanalyl cyclase receptors |
a. There would be no conformational change in the receptor, and it would not bind to the Gα subunit. | ||
b. The Gα subunit's GTP would never be hydrolyzed. | ||
c. There would be no activation of the Gα subunit, and it would not bind to its effector. | ||
d. The Gα subunit would not undergo a conformational change, so it would not disassociate from its GDP. |
a. There would be no conformational change in the Gα subunit, so it would never disassociate from the β and γ subunits. | ||
b. The Gα subunit would always be active, so it would perpetually activate its effector. | ||
c. There would be no activation of the Gα subunit, and it would not bind to its effector. | ||
d. The Gα subunit would not undergo a conformational change, so it would not disassociate from its GDP. |
a. Cells produce signaling molecules of which they themselves are the targets. | ||
b. The ligand on a cell's surface binds to the receptor of a cell directly adjacent to it. | ||
c. Molecules released elsewhere in the body are transported by the circulatory system to target cells. | ||
d. Cells release a signal molecule that reaches nearby target cells. |
a. They are involved in a signaling cascade whose result is induced cell death. | ||
b. They are also known as members of the TGF-β family. | ||
c. They are the primary receptors involved in activating growth factors. | ||
d. They catalyze the formation of GMP, a secondary messenger. |
a. They are involved in nuclear protein transport and vesicle trafficking. | ||
b. They behave in a manner analogous to that of the Gα subunit of G proteins but are not associated with βγ subunits. | ||
c. Mutations in these proteins often lead to excessive cell growth and proliferation in cancer cells. | ||
d. Typical mutations in these proteins prevent them from hydrolyzing the GTP to which they have bound. |
a. Cells produce signaling molecules of which they themselves are the targets. | ||
b. The ligand on a cell | ||
c. Molecules released elsewhere in the body are transported by the circulatory system to target cells. | ||
d. Cells release a signal molecule that reaches nearby target cells. |
a. G-protein-coupled receptors | ||
b. Receptor tyrosine kinases | ||
c. Cytokine receptors | ||
d. Guanalyl cyclase receptors |
a. Selectins | ||
b. Integrins | ||
c. Immunoblogins (Ig-CAMs) | ||
d. All of these |
a. Cadherins | ||
b. Integrins | ||
c. Immunoblogins (Ig-CAMs) | ||
d. All of these |
a. Gap junctions | ||
b. Tight junctions | ||
c. Desmosomes | ||
d. Adherens junctions |
a. Gap junctions | ||
b. Tight junctions | ||
c. Desmosomes | ||
d. Adherens junctions |
a. a higher proportion of fibrous proteins. | ||
b. a matrix hardened with calcium-phosphate crystals. | ||
c. a high number of elastin fibers. | ||
d. a higher proportion of polysaccharides forming a firm, supportive gel. |
a. a higher proportion of fibrous proteins. | ||
b. a matrix hardened with calcium-phosphate crystals. | ||
c. a high number of elastin fibers. | ||
d. a higher proportion of polysaccharides forming a firm, supportive gel. |
a. a higher proportion of fibrous proteins. | ||
b. a matrix hardened with calcium-phosphate crystals. | ||
c. a high number of elastin fibers. | ||
d. a higher proportion of polysaccharides forming a firm, supportive gel. |
a. a higher proportion of fibrous proteins. | ||
b. a matrix hardened with calcium-phosphate crystals. | ||
c. a high number of elastin fibers. | ||
d. a higher proportion of polysaccharides forming a firm, supportive gel. |
a. hemicellulose. | ||
b. pectin. | ||
c. glycogen. | ||
d. cellulose. |
a. Collagens | ||
b. Elastins | ||
c. Proteoglycans | ||
d. Adhesive proteins |
a. Disruption of actin-filament formation | ||
b. Disruption of microtubule formation | ||
c. Disruption of intermediate-filament formation | ||
d. None of these |
a. Disruption of actin-filament formation | ||
b. Disruption of microtubule formation | ||
c. Disruption of intermediate-filament formation | ||
d. None of these |
a. It could increase the concentration of GTP in the cell. | ||
b. It could prevent microtubule polymerization. | ||
c. It could prevent MAP activity. | ||
d. It could do all of these. |
a. The bleached zone would move from the plus end toward the minus end of the filaments, indicating that actin filaments are in a continual state of assembly/disassembly. | ||
b. The bleached zone would quickly disappear, indicating that actin-binding proteins quickly repair damaged portions of actin filaments. | ||
c. The bleached zone would remain steady within the filaments, indicating that actin filaments are in a continual state of assembly/disassembly. | ||
d. The bleached zone would remain in the same place within the filaments, indicating that actin filaments are very stable. |
a. Muscle contraction would be promoted, because calcium increases the speed at which ATP binds to the myosin head. | ||
b. Muscle contraction would be inhibited, because calcium triggers the conformation change in the shape of the myosin head. | ||
c. Muscle contraction would be inhibited, because calcium shifts the proteins bound to actin to a different position, allowing actin to contract. | ||
d. Muscle contraction would be promoted, because calcium triggers the binding of proteins to actin, preventing it from contracting. |
a. Actin filaments must be polymerized and cross-linked, so the front of the cell can extend forward. | ||
b. Focal adhesions or other attachments must be made between the back end of the cell and its substrate. | ||
c. Protrusions, for example lamellipodia, must be pulled back into the cell so that they will not block its movement. | ||
d. Sarcomeres must contract to bring the cell forward. |
a. Both are involved in cell movement. | ||
b. Both are involved in anchoring cells to substrates. | ||
c. Both are polymers of single types of proteins. | ||
d. Both are nonpolar molecules. |
a. The assembly of both is polymerized by ATP. | ||
b. Both are highly stable molecules. | ||
c. Both exhibit dynamic instability. | ||
d. Both are nonpolar molecules. |
a. Once it has formed large filaments, those filaments have a binding site with a very high affinity for actin-disassembly proteins. | ||
b. Actin does not have a high turnover in cells; it is very stable. | ||
c. Its assembly with ATP triggers the hydrolysis of ATP, which in turns makes the ADP-bound actin more likely to disassemble. | ||
d. Its loose cross-linkage makes its filament connections fragile and easily disrupted. |
a. DNA methylation | ||
b. Chromatin condensation | ||
c. Binding of transcription factors to enhancers | ||
d. Binding of repressors to activator proteins |
a. Both are transcribed at very rapid rates. | ||
b. Both have been moved out of the nuclear envelope. | ||
c. Both are no longer in association with proteins. | ||
d. Both are highly condensed so that transcription is impossible. |
a. The inner nuclear membrane | ||
b. The nucleolus | ||
c. The nuclear lamina | ||
d. The nuclear pore complex |
a. The inner nuclear membrane | ||
b. The nucleolus | ||
c. The nuclear lamina | ||
d. The nuclear pore complex |
a. DNA Methylation | ||
b. Chromatin condensation | ||
c. Transcriptional activation | ||
d. Transcriptional repression |
a. The way chromosomes take up dye is consistent and predictable regardless of where genes appear within them. | ||
b. Genes have an affinity for certain dyes, so they aggregate in such areas during chromosome condensation. | ||
c. The way that chromosomes organize DNA is predictable and reproducible each time they condense during metaphase. | ||
d. The way that chromosomes condense repeats the formation of heterochromatin. |
a. Histone acetyltransferases, which acetylate histones | ||
b. Histone deacetylases, which de-acetylate histones | ||
c. Nucleosome remodeling factors, which change the structure of nucleosomes | ||
d. A and C are both examples of transcriptional repressors. |
a. Enhancers can stimulate transcription from more than one promoter. | ||
b. Enhancers can stimulate transcription from an upstream or downstream location. | ||
c. Enhancers can stimulate transcription, even when located a long distance from a promoter. | ||
d. Enhancers can stimulate transcription when in a forward orientation and suppress transcription when in a backward orientation. |
a. The small subunit of eukaryotic ribosomes is composed of one type of rRNA and approximately 30 proteins. | ||
b. The self-assembly of ribosomes in vitro does not occur effectively in the absence of rRNAs, even with all ribosomal proteins present. | ||
c. Ribosomes created by self-assembly in vitro continue to function in the absence of many ribosomal proteins when rRNAs are present. | ||
d. The ribosomal subunit is able to form peptide bonds if rRNAs are present, even when the vast majority of ribosomal proteins are absent. |
a. Prometaphase | ||
b. Metaphase | ||
c. Anaphase | ||
d. Telophase |
a. Prophase | ||
b. Prometaphase | ||
c. Metaphase | ||
d. Telophase |
a. Cytokinesis | ||
b. Prophase | ||
c. Anaphase | ||
d. Telophase |
a. Cytokinesis | ||
b. Prophase | ||
c. Anaphase | ||
d. Telophase |
a. Prophase | ||
b. Prometaphase | ||
c. Metaphase | ||
d. Telophase |
a. Prophase | ||
b. Prometaphase | ||
c. Metaphase | ||
d. Telophase |
a. Vesicles with cell-wall components fuse at the site of the metaphase plate, and the resultant disc eventually expands to fuse with the original plasma membrane and cell wall, forming two separate cells. | ||
b. An outgrowth of the cell wall and plasma membrane, the "septum," grows from opposite sides of the membrane toward the middle of the cell, where the two septa meet and fuse, creating two separate cells. | ||
c. A ring of actin and myosin filaments contracts the plasma membrane, eventually pinching the cell and dividing it in two. | ||
d. None of these occurs in bacterial cells. |
a. Prometaphase | ||
b. Metaphase | ||
c. Anaphase | ||
d. Telophase |
a. Cytokinesis | ||
b. Prophase | ||
c. Anaphase | ||
d. Telophase |
a. Leptotene | ||
b. Zygotene | ||
c. Pachytene | ||
d. Diplotene |
a. Leptotene | ||
b. Zygotene | ||
c. Pachytene | ||
d. Diakinesis |
a. Leptotene | ||
b. Zygotene | ||
c. Pachytene | ||
d. Diakinesis |
a. The first meiotic division | ||
b. The second meiotic division | ||
c. Mitosis | ||
d. Differentiation and maturation |
a. Homologous chromosomes separate. | ||
b. Sister chromatids separate. | ||
c. Bivalent chromosomes align on the spindle. | ||
d. Chromosomes decondense. |
a. Homologous chromosomes separate. | ||
b. Sister chromatids separate. | ||
c. Bivalent chromosomes align on the spindle. | ||
d. Chromosomes decondense. |
a. Homologous chromosomes pair. | ||
b. At metaphase, both kinetochores of one homologue face the same pole. | ||
c. Chiasmata link homologous chromosomes. | ||
d. DNA replication occurs prior to initiation of the process. |
a. They do not have an important role once desynapsis has occurred. | ||
b. They hold the chromosomes together, ensuring their alignment at metaphase. | ||
c. They orient the chromosomes | ||
d. They allow recombination to occur at recombination nodules. |
a. Meiosis is the most common type of cell division and occurs at a much higher rate than mitosis. | ||
b. The re-assortment of alleles during meiosis guarantees that only the best allelic combinations will be present in the next generation. | ||
c. The reshuffling of alleles and recombination in meiosis lead to phenotypic variation, which is better for a species' survival in a changing environment. | ||
d. Sexual reproduction and meiosis are not considered evolutionarily beneficial, but once they are present in a species they are too hard to select against. |
a. G1 | ||
b. G2 | ||
c. S | ||
d. M |
a. CKIs, such as p27, bind to CDK and cyclin, and through conformational changes, CKIs lock them in the inactive state. | ||
b. Cyclins, which activate CDK-cyclins and are rapidly produced and broken down, are allowed to degrade naturally without more molecules being produced. | ||
c. CAKs phosphorylate a residue on the CDK | ||
d. Cyclins are actively degraded within the nucleus, so they are not present at a high enough volume to activate CDK-cyclins. |
a. Primarily in G2 | ||
b. Primarily in G0 | ||
c. In phases in M and S | ||
d. In phases M, G1, S, and G2 |
a. Primarily in G2 | ||
b. Primarily in G0 | ||
c. In phases in M and S | ||
d. In phases M, G1, S, and G2 |
a. Primarily in G2 | ||
b. Primarily in G0 | ||
c. In phases in M and S | ||
d. In phases M, G1, S, and G2 |
a. Unphosphorylated, repressing E2F | ||
b. Hypophosphorylated, repressing E2F | ||
c. Hyperphosphorylated, unable to repress E2F | ||
d. Hyperphosphorylated, repressing E2F |
a. Unphosphorylated, repressing E2F | ||
b. Hypophosphorylated, repressing E2F | ||
c. Hyperphosphorylated, unable to repress E2F | ||
d. Hyperphosphorylated, repressing E2F |
a. There is a restriction point for G1, and it occurs around 10 hours after growth factors are added to cells. | ||
b. There is a restriction point for G1, and it occurs around 14 hours after growth factors are added to cells. | ||
c. There is a restriction point for G1, and it occurs around 16 hours after growth factors are added to cells. | ||
d. There is no restriction point for G1 once growth factors have been added to cells. |
a. Because there is a clear restriction point during G1 to initiate cell growth, cyclin D is not needed during this phase. | ||
b. Cyclin D is required only at the very beginning of the G1 phase. | ||
c. Cyclin D is required at every point within the G1 phase. | ||
d. Cyclin D is required to get cells past the restriction point in G1, after which cell growth will continue regardless. |
a. Proteins that were brought into the nucleus would remain bound to importin indefinitely. | ||
b. Proteins that were destined for the nucleus would never be bound to importin and would remain outside it indefinitely. | ||
c. Proteins that were destined for the nucleus would never be brought, by importin, to the nuclear pore. | ||
d. This change in the function of the α subunit would not affect proteins destined for the nucleus. |
a. Proteins that were brought into the nucleus would remain bound to importin indefinitely. | ||
b. Proteins that were destined for the nucleus would never be bound to importin and would remain outside it indefinitely. | ||
c. Proteins that were destined for the nucleus would never be brought, by importin, to the nuclear pore. | ||
d. This change in the function of the α subunit would not affect proteins destined for the nucleus. |
a. Proteins that were brought into the nucleus would remain bound to importin indefinitely. | ||
b. Proteins that were destined for the nucleus would never be bound to importin and would remain outside it indefinitely. | ||
c. Proteins that were destined for the nucleus would never be brought, by importin, to the nuclear pore. | ||
d. Protein transport would continue normally, as this is the normal location for these enzymes. |
a. COP I coated vesicle | ||
b. Dynamin vesicle | ||
c. COP II coated vesicle | ||
d. Caveolin-coated vesicle |
a. COP I coated vesicle | ||
b. Clathrin-coated vesicle | ||
c. COP II coated vesicle | ||
d. Caveolin-coated vesicle |
a. Protein translocation | ||
b. Protein folding | ||
c. Glycosylation | ||
d. Protein degradation |
a. Rough ER lumen | ||
b. Mitochondrial matrix | ||
c. Chloroplast stroma | ||
d. Nucleus |
a. Transport of proteins to chloroplasts is even more difficult than to mitochondria, because chloroplasts have three membranes, not two. | ||
b. While proteins targeted to mitochondria have positively charged presequences, the transit peptides of chloroplasts are not charged. | ||
c. While protein transport in mitochondria requires chaperone proteins on the outside and inside of the organelle, protein transport in chloroplasts only requires outside chaperones. | ||
d. As with mitochondria, specific proteins from the cytosol must be transferred to the chloroplast. |
a. The proteins involved in oxidative metabolism must be transferred from the cytosol to mitochondria. | ||
b. The proteins involved in expressing mitochondrial DNA must be transferred from the cytosol to mitochondria. | ||
c. Protein transport to mitochondria is made more difficult because of the double membrane of mitochondria. | ||
d. Proteins that are brought into mitochondria by Hsp70 chaperones enter the matrix in a pre-folded state. |
a. Glyoxysome | ||
b. Peroxysome | ||
c. Lysosome | ||
d. Golgi apparatus |
a. Peroxisome | ||
b. White-fat mitochondria | ||
c. Smooth ER | ||
d. Brown-fat mitochondria |
a. There is nothing to prevent these enzymes from degrading cytoplasmic elements, which is why the membrane of the lysosome is designed so that it can be immediately repaired of damage. | ||
b. These hydrolases only function at a lower pH than is present in the cytoplasm, so they would not be able to work outside the lysosome. | ||
c. There are repressor-proteins present in the cytoplasm that bind to these hydrolases and inactivate them. | ||
d. Hydrolases only bind to and degrade aging molecules and organelles that have a specific amino-acid sequence; they would not degrade healthy cytoplasmic elements. |
a. Golgi apparatus | ||
b. Chloroplast | ||
c. Smooth ER | ||
d. Mitochondria |
a. Glyoxysome | ||
b. Peroxysome | ||
c. Lysosome | ||
d. Golgi apparatus |
a. Glyoxysome | ||
b. Peroxysome | ||
c. Lysosome | ||
d. Golgi apparatus |
a. Golgi apparatus | ||
b. Chloroplast | ||
c. Smooth ER | ||
d. Mitochondria |
a. Peroxisome | ||
b. White-fat mitochondria | ||
c. Smooth ER | ||
d. Brown-fat mitochondria |
a. Peroxisome | ||
b. White-fat mitochondria | ||
c. Smooth ER | ||
d. Brown-fat mitochondria |
a. The inner membrane of each is responsible for oxidative phosphorylation. | ||
b. Both contain their own genetic material. | ||
c. Both contain inner and outer membranes. | ||
d. Both contain metabolic enzymes responsible for oxidative metabolism. |
a. extrinsic pathway. | ||
b. intrinsic pathway. | ||
c. death-inducing signaling pathway. | ||
d. necrotic pathway. |
a. Caspase -7 | ||
b. Caspase-6 | ||
c. Caspase-1 | ||
d. Caspase-8 |
a. DNA fragmentation | ||
b. Shrinkage of the cytoplasm | ||
c. Lysis or damage to neighboring cells | ||
d. Membrane changes |
a. Phosphatidylserine | ||
b. Phosphatidylcholine | ||
c. Phosphatidylinositsol | ||
d. Diacylglycerol |