WorksheetsBIOCHEM MIDTERM QUIZ COMPILATION
Total questions: 160
Worksheet time: 1hrs 20mins
How many carbon atoms do most common monosaccharides have?
• 2 to 4
• 3 to 7
• 2 to 8
• 3 to 6
Of all the types of lipid, which ones are based on fused rings?
• Eicosanoids
• Steroids
• Phosphoglycerides
• Sphingolipids
In the biological world, glucose is the most abundant ____.
• D-aldohexose
• L-ketohexose
• L-aldohexose
• D-ketohexose
Micelles of fatty acids in water are organized such that the ______ face the solvent and the ______ are directed toward the interior.
• hydrophilic heads… hydrophobic tails
• hydrocarbon chains… carboxylic acid groups
• carboxylic acid groups… hydrogen chains
• hydrophobic tails… hydrophilic heads
5. A medical condition characterized by an elevated or high amount of glucose in the blood.
• hypoglycemia
• hypothermia
• hyperglycemia
• hypercholesterolemia
The hydroxyl group in a β-glucose is above the anomeric carbon in the Haworth projection because it's ______ of carbon in the Fischer projection.
• at the left
• at the right
• on top
• at the middle
Which of these statements is incorrect about the displayed structural formula of a chemical species?
• It contains a glycerol backbone.
• It is a prominent part of cell membranes.
• It has nonpolar "tails" and polar "heads"
• It is a major form of energy storage.
1. Prostaglandins are lipids that cause the sensation of pain. What enzymes catalyze the synthesis of Prostaglandins from arachidonic acid?
• Prostaglandase
• Arachidonase
• Eicosanoidase
• Cyclooxygenase
10. What particles are formed after the lipid is removed from the VLDL core that increases their density?
• VLDL
• HDL
• LDL
• VHDL
One of the most prevalent forms of D-ribose and other pentoses in the biological world
What condition can trigger the COX-2 enzyme to catalyze the synthesis of prostaglandins from arachidonic acid?
• Inflammation
• Muscle contraction
• Starvation
• Dehydration
What constitute the highest proportion of liquid triglycerols or oils?
• proteins
• cholesterol
• saturated fatty acids
• unsaturated fatty acids
Which biological molecule is neither considered a macromolecule nor a polymer of monomers?
• Carbohydrate
• Lipid
• Nucleic acid
• Protein
They are 100 times more potent than histamine being able to produce muscle contractions, especially in the lungs resulting in an asthma-like attack.
• Prostaglandins
• Leukotrienes
• Thromboxanes
• Bradykinins
Which of these statements best explains why trans fats are detrimental to health?
• Trans fats consist of artificial oils and preservatives.
• Trans fats have a longer shelf life than other lipids.
• Trans fats stay longer than other lipids in the bloodstream.
• Trans fats are highly hydrogenated to have a delectable taste
Identify the most accurate name of the chemical structure shown below.
• α-D-Glucopyranose
• α-D-Glucofuranose
• β-D-Glucopyranose
• β-D-Glucofuranose
Prostaglandins, thromboxanes, and leukotrienes are compounds formed during inflammation. They are all produced from arachidonic acid. What term best applies to arachidonic acid?
• Antecedent
• Precursor
• Progenitor
• Predecessor
The triacylglycerols found in plants are more __________ than those in animals.
• monounsaturated
• polyunsaturated
• polysaturated
• monosaturated
Where are HDLs synthesized?
• intestine
• liver
• stomach
• pancreas
The Haworth projection of ribose forms a _______.
• furanose ring
• pyranose ring
• stachyose ring
• raffinose ring
Which lipid molecule is an important precursor for the synthesis of estrogen and many other hormones?
• Glycerol
• Cholesterol
• Ceramide
• Sphingolipid
Which lipoprotein transports cholesterol from extra hepatic tissues to the liver?
• VHDL
• HDL
• LDL
• Chylomicrons
Different classes of lipids may include molecules having very different functional groups. Which characteristic is common to all lipids?
• soluble in polar organic solvents
• soluble in nonpolar organic solvents
• soluble when hydrogenated
• soluble in hot water or aqueous solution
What lipoprotein must be present at a higher level in the blood plasma of a healthier individual?
• HDL
• LDL
• VLDL
• Chylomicron
Which of these illustrated Haworth projection of monosaccharides is the resulting Beta (β) version derived from the Fischer Projection of a monosaccharide below?
• A
• B
• C
• D
The following are polysaccharides except
• cellulose.
• hemicellulose.
• amylopectin.
• aldose.
Which is most applicable to the naturallyoccurring fatty acids?
• They have the trans-configuration
• They have the α- conformation
• They have an odd number of carbon atoms.
• They have an even number of carbon atoms.
The common six-carbon sugars (hexoses) are D-glucose, D-fructose, D-galactose, and Dmannose. Which one is a ketohexose?
• D-fructose
• D-galactose
• D-glucose
• D-mannose
The following are closely associated with carbohydrates except
• heparin
• hyaluronic acid
• glucuronic acid
• glutamic acid
Which fats are the most abundant in coconut oil that other scientists classified unhealthy oil?
• Omega-6 fats
• Polyunsaturated fats
• Saturated fats
• Omega-3 fats
The melting properties of fatty acids and lipid bilayers is primarily due to the
• Hydrogen bonds.
• London dispersion forces.
• Hydrophobic interactions.
• Electrostatic interactions.
. Which of these combinations is accurate?
• Fructose + Galactose ----> Lactose
• Fructose + Fructose ----> Sucrose
• Glucose + Fructose ----> Maltose
• Glucose + Glucose ---> Maltose
Which of these factors has no effect on the melting points of fatty acids?
• the length of the carbon chains
• the number of chemical bonds
• the type of double bonds (cis/trans)
• the number of nitrogen atoms
Human's and cow's milk consist of disaccharides D-Galactopyranose and DGlucopyranose. Which bond links these two compounds?
• β-1,6-glycosidic bond
• β-1,4-glycosidic bond
• α-1,4-glycosidic bond
• α-1,6-glycosidic bond
Both thromboxanes and leukotrienes are complex lipids. How do they differ structurally?
Leukotrienes are linear, while thromboxanes have a cyclic portion in their structure.
Leukotrienes have many physiological activities while thromboxanes have only a few functions.
Leukotrienes play a role in platelet aggregation while thromboxanes mitigate allergic reactions.
Leukotrienes are directly inhibited by COX enzymes while thromboxanes are stopped
The levels of lipoprotein indicate a symptom of faulty cholesterol transport and a warning of possible atherosclerosis
• high LDL together with high HDL
• low LDL together with low HDL
• low LDL together with high HDL
• high LDL together with low HDL
Different classes of lipids may include molecules having very different functional groups. Which characteristic is common to all lipids?
• soluble in nonpolar organic solvents
• soluble in inorganic solvents
• soluble when hydrogenated
• soluble in very hot water
Biological molecules that are made of the same elements (CHO), but have different structures; thus they have different biological and chemical properties
• carbohydrates and lipids
• proteins and lipids
• carbohydrates and proteins
• nucleic acids and proteins
Cutin, the waxy coating of plants leaves, is a chemical compound that belongs to which biological molecule?
• Carbohydrates
• Proteins
• Lipids
• Nucleic acids
The areas on a cell membrane that have high concentrations of LDL receptors and participate in transporting the LDLs into the cell.
• Coated vesicles
• Coated pits
• Coated receptors
• Coated peripheral tissues
Which of these descriptions is the effect of cis configuration of the double bonds to the fatty acid?
• Its hydrocarbon chains have a less ordered structure resulting in liquid fatty acid.
• The fatty acid has obtained a melting point that is above room temperature.
• Its hydrocarbon chains have become rigidly packed resulting in liquid fatty acid.
• The strong London dispersion forces between carbons results in solid fatty acid.
Lactose intolerance is the inability of many higher mammals to hydrolyze this type of bond between galactose and glucose molecules.
• phosphodiester bond
• hydrogen bond
• β-glycosidic bond
• α-glycosidic bond
Which drug has been known to slow down the synthesis of the thromboxanes by inhibiting the COX enzyme?
• Ciprofloxacin
• Cefalexin
• Aspirin
• Thrombin
. Unsaturated fatty acids are typically liquid at room temperature because their hydrocarbons are ______ arranged due to their ______ bonds.
• tightly… double
• tightly… triple
• loosely… single
• loosely… double
In the Fischer projection of D-glucose, which carbon is not a stereocenter?
• 1
• 2
• 3
• 4
• 5
Which of the following shows the structural difference between saturated and unsaturated fatty acid molecules?
• the total number of carbons
• the presence of double bond/s
• the solubility of the fatty acids
• the melting point of fatty acids
Of these given molecules, which is a ribose with an L designation?
A
B
C
D
. Identify the yield when NaBH4 reduces each aldehyde carbonyl.
• primary alcohol
• secondary alcohol
• tertiary alcohol
all options are correct
The designations D and L refer to the configuration of the stereocenter closest to the aldehyde or ketone group on a monosaccharide chain.
• True
• False
A mutation of steroid hormone converted it from nonpolar to a polar molecule. How would this affect its function?
• The polar hormone would not be able to pass through the cell membrane to reach its target.
• The polar hormone would be able to travel faster in the bloodstream to reach its target.
• The polar hormone would get stuck in the cell membrane's hydrophobic layer of phospholipid bilayer.
• The polar hormone would not be released by the secreting glands and could not reach its target.
Heparin, a compound pharmacologically used as a blood thinner, belongs to which type of biological molecule?
• carbohydrate
• lipid
• protein
• nucleic acid
Fat is important as a storage molecule. It can provide protection to vital organs as well as warmth. In what form are lipids most commonly stored?
• cholesterol
• lipoproteins
• triacylglycerides
• glycerols
It is the carbon that was the carbonyl carbon in the open-chain form (Fischer projection) of the monosaccharide.
• hemiketal carbon
• alpha carbon
• chiral carbon
• anomeric carbon
Which structural formula pertains to the only group of lipids with conjugated double bonds?
A
B
C
D
. Our cell membranes exist as bilayers largely due to phospholipids that form these bilayers of the hydrophilic phosphate heads and hydrophobic fatty acid tails. What term is used to define this characteristic of phospholipid?
• Amphoteric
• Amphiprotic
• Amphipathic
• Amphophillic
Which of these descriptions is the effect of cis configuration of the double bonds in unsaturated fatty acid?
• Its hydrocarbon chains have a less ordered structure resulting in liquid fatty acid.
• The strong London dispersion forces between carbons results in solid fatty acid.
• The fatty acid has obtained a melting point that is above room temperature.
• Its hydrocarbon chains have become rigidly packed resulting in liquid fatty acid.
D-glucose is the most abundant hexose in the biological world. It is also known as
• raffinose.
• stachyose.
• triose.
• dextrose
Hydrogenation of an unsaturated fatty acid usually results in a compound having
• decreased melting point.
• increased melting point.
• repulsive rancid smell.
• stabilized cis configuration
. Melting points of fatty acids increases as the number of carbons in the hydrocarbon chains _________ and as the number of double bonds ________.
• decreases… decreases
• decreases… increases
• increases... decreases
• increases… increases
The tertiary structure of the protein is stabilized in 4 ways. Which one does not stabilize protein molecules?
• hydrophobic interaction
• metallic bond
• hydrogen bond
• salt bridge
In the formation of the Haworth projection in monosaccharides, carbon 1
• is the carbon in CH2OH of Fischer projection
• is the carbonyl carbon on topmost of Fischer projection
• is the carbonyl carbon on the bottom of Fischer projection
• is the anomeric carbon of the Fischer projection
It is the simplest and the basic level of structure of protein made of a linear sequence of amino acids in a polypeptide chain.
• primary
• original
• fundamental
• elemental
Adult hemoglobin has 2 alpha chains of 141 amino acids each and 2 beta chains of 146 amino acids each. How many amino acids are there in an adult hemoglobin molecule?
• 574
• 292
• 282
• 679
Amino acids are sometimes written in their unionized form. What does un-ionized form mean?
• neutral pH
• charged
• uncharged
• polar
It is known as the simplest of all amino acids due to its side chain that contains only a Hydrogen atom.
• Serine
• Glycine
• Alanine
• Proline
Which set of descriptions best describes the tertiary level structure of a protein?
• repeated folding of β-sheets or α- helices
• 3-dimensional, compact and globular
• packed variable subunits forming large complexes
• a long linear sequence of amino acids
Which of these descriptions does NOT describe a denatured protein?
• intact primary structure
• lost functionality
• distorted shape
• increased solubility
At the isoelectric point (pI) of proteins the negative and positive charges are balanced reducing repulsive electrostatic forces and the attraction forces predominate causing proteins to _____ and precipitate out.
• repulse
• aggregate
• disperse
• dissolve
The only achiral amino acid
• Isoleucine
• Glycine
• Proline
• Threonine
Salt bridges are shown by the attraction of the - NH3+ group of lysine and the -COO- group of aspartic acid. Which one is synonymous to salt bridges?
• Covalent bonding
• Hydrophobic interaction
• Hydrophilic interaction
• Electrostatic attraction
Amino acids are linked together by the peptide bond between the ___ group of one amino acid and the ___ group of another amino acid.
• carbon of carboxyl… nitrogen of the amino
• alpha carbon.. nitrogen of side chain
• carbon of carbonyl… nitrogen of the amino
• nitrogen of carboxyl… carbon of the amino
Where is amino acid's side chain bonded to?
• Hydrogen atom
• alpha carbon
• carboxyl group
• amino group
Which structure does Tropocollagen, the triple helix form of collagen, demonstrate?
• quaternary
• tertiary
• primary
• secondary
What amino acids are bonded by peptide bonds in the illustration that follows?
• Valine and Phenylalanine
• Methionine and Isoleucine
• Cysteine and Tyrosine
• Arginine and Lysine
What makes amino acid Glycine polar?
• amino & carboxyl groups
• the alpha carbon and hydrogen
• the uneven distribution of H atoms
• amino & carbonyl group
The amino acids in this displayed tripeptide
• Met-Leu-Phe
• Glu-Thr-Cys
• Met-Ser-Cys
• Lys-Asn-Ala
One hydrophobic amino acid has a very unique structure compared to other amino acids. What makes it very unique?
• Its side chain is bonded to α-carbon and to an amino group.
• Its side chain in bonded to α-carbon and to carboxyl group.
• It is has polar side chain, but uncharged.
• It has nonpolar side chain, but ucharged.
Fibrous proteins are water-insoluble. Due to this characteristic which fibrous protein function in organisms is correct?
• transport
• structural
• catalysis
• storage
It is an amino acid present in milk that helps induce sleep. This fact is the source of an urban myth that drinking a glass of warm milk at bedtime makes us fall asleep.
• Isoleucine
• Threonine
• Tryptophan
It is an example of a protein having a globular shape or conformation.
• keratin
• tropocollagen
• hemoglobin
• myosin
Proteins are least soluble in water at their isoelectric point. Hence proteins can be separated from the solution at this pH because proteins form _____.
• homogenate
• filtrate
• precipitate
• sublimate
These are the amino acids that have a second stereocenter.
• Isoleucine and Threonine
• Serine and Tyrosine
• Lysine and Tryptophan
• Proline and Glycine
Which of these properties is directly associated with the Isoelectric point (pI) of protein?
• polarity
• pH
• electric charge
• solubility
What is the closest pH of each of the several amino acids when it has almost equal or the same positive and negative charges?
• pH 6
• pH 14
• pH 7
• pH 0
Which amino acids are shown by the tripeptide below?
• Threonine-Methionine-Asparagine
• Alanine-Glutamine-Cysteine
• Alanine-Glutamic acid-Cysteine
• Threonine-Arginine-Methionine
Glycine amino acid is an odd case and most literature conflicts on its proper designation. Glycine, as a compound, behaves like a polar amino acid largely because of the influence of the α-amino and α-COOH groups. What makes glycine nonpolar?
• Hydrogen in the amino group
• Methyl side chain
• Hydrocarbon side chain
• Hydrogen atoms side chain
Which organisms have an identical sequence of amino acids for alpha chain at positions 8-9-10 in protein insulin?
• human and hog
• human and cow
• cow and hog
• hog and sheep
What makes the 20 amino acids different from one another?
• carboxyl group
• stereocenter
• side chain
• amino group
Which amino acids have 0 net charge when their pH is around or too close pH 10.
• Arginine & Lysine
• Arginine & Histidine
• Aspartic acid & Glutamic acid
• Alanine & Proline
The hormone insulin is made of 2 polypeptide chains held together by 2 interchain disulfide bonds. Which of these expressions represents a disulfide bond?
• SO2 - SO2
• S - O - S
• SO - SO
• S - S
At pH 10 or higher what is the net electrical charge of the majority of the amino acids?
• -1
• 0
• +1 and -1 (zwitterion)
• +1
The secondary structure of a protein is formed when amino acids sequence are linked by ____ bonds.
• Hydrogen
• Carbon
• Peptide
• Amide
Pure ethanol (100% concentration) is less effective than 70% EtOH.
• It has 30% water that are bonded to one another making water less volatile.
• It penetrates slowly the bacterial cell membrane allowing the bacteria to escape.
• Its polarity hinders pure alcohol to permeate the lipid bilayer of bacterial cell membrane.
• It denatures bacterial membrane so fast forming a protective layer against more alcohol entry
Which are not considered as denaturing agents or compounds?
• 0.9 % saline solution and distilled water
• heavy metals and reducing agents
• alcohol and acetone
• strong acids and alkalis
By convention, R stands for the chemical group attached to the basic structure of amino acid. What does R stand for in the structural formula of amino acids?
• functional group
• alkyl group
• hydroxyl chain
• side chain
It is a molecule that has both positively and negatively charged functional groups but the net charge of the entire molecule is zero.
• zwitterion
• polar
• non-polar
• carbocation
the level of protein structure that remains undistorted or unchanged by denaturing agents
• secondary
• tertiary
• primary
• quaternary
The native conformation or normal form of a protein predominantly consists of alpha helix, while the variant/mutant has beta structure. The beta structure consists more hydrophobic groups that significantly lack a polar outer layer. Having this information, how could we differentiate between the normal and mutant protein in the lab?
• Denature both samples through heat. Normal protein gets denatured while the variant stay intact.
• Count the number of amino acids. The native protein contains more amino acids than the variant.
• Weigh the 2 protein samples. Heavier mass is shown by the variant while native one is much lighter.
• Dissolve both sample proteins in water. Normal protein dissolves while mutant or variant does not.
Water is a reactant that hydrolyzes the two amide bonds in urea. The enzyme involved in this reaction is categorized as _____.
• urease
• transferase
• hydrolyase
• hydrolase
Enzymes catalyze the cleavage or cutting of bonds, usually esters and amides, with water. These are called hydrolysis reactions. Which enzymes are involved?
• peptidases
• Hydrolases
• Esterases
• Dehydrolases
Water is a reactant that hydrolyzes the two amide bonds in urea. The enzyme involved in this reaction is categorized as _____.
• hydrolyase
• transferase
• urease
• hydrolase
In noncompetitive inhibition, how does the inhibitor change the conformation of the active site?
• By binding to a part of the enzyme other than the active site
• By creating another active site for an enzyme
• By binding to the active site of an enzyme
• By binding to a part opposite to the enzyme's active site
The vitamin involved in the coenzyme function of decarboxylation reactions
• Thiamine
• Biotin
• Riboflavin
• Niacin
In enzyme allosteric mechanism, R state means “relaxed" state of an enzyme. Which one describes this condition?
• high-activity and high-affinity
• low-activity and high affinity
• high activity and low affinity
• low-activity and low-affinity
Which situation has been observed to result in saturation curve that levels off or stagnate the activity of enzymes?
• increasing the pH of the solution
• increasing substrate concentration
• increasing enzyme concentration
• increasing the temperature
The activation energy in an enzyme-catalyzed reaction is higher than the activation energy in an uncatalyzed reaction, which is why a catalyzed reaction proceeds at a faster rate.
• True
• Depending on enzyme
• Depending on substrate
• False
The antiviral drug Tipranavir has no obvious structural similarity to a protein substrate. It is used to treat HIV, by binding to viral proteases thus blocking the activity of a viral enzyme that helps the virus make more copies of itself. This is an example of _______.
• noncompetitive inhibition
• competitive inhibition
• allosteric effect
• induced-fit mechanism
Aspartase catalyzes the addition of a functional group to a double bond. The enzyme in this reaction is categorized as a/an ____.
• Asparaginase
• lyase
• dipeptidase
• Aspartase
Which of the options is true of the induced-fit model of enzyme catalysis?
• The initial binding of enzyme and substrate is the most tightly bound conformation.
• The active site can be influenced by molecules binding elsewhere on an enzyme.
• All responses are correct.
• The induced fit must occur before the initial binding of enzyme and substrate for reaction to proceed.
Certain bacterial enzyme is more active in a temperature range of 39oC- 41oC. Which of these descriptions holds true about the activity of this bacterial enzyme?
• decreases if the patient's temperature decreases to 35 °C.
• nonfunctional due to the denaturation process at 40 °C
• increases if the patient's temperature decreases to 35 °C.
• much more functional at temperature beyond 41 °C
Per PPT slide on enzyme kinetics, which graph achieves the maximum rate of reaction despite the presence of inhibiting compound?
B
A
C
A,. B, and C
Which molecule is also formed when amino acids are bonded by peptide bonds?
• carbon dioxide (CO2)
• hydronium ion (H3O+)
• ammonia (NH3)
• water (H2O)
Succinate is oxidized and FAD is reduced. The enzyme involved is classified as a/an _______.
• reductase
• oxidoreductase
• oxidase
• succinase
The reactant and product have the same molecular formula, but they have different molecular structures, so they are isomers. The enzyme that catalyzes the reaction is classified as a/an ______.
• lyase
• isomerase
• chiralase
• transferase
Trypsin and chymotrypsin are enzymes that catalyze the hydrolysis of amide bonds in proteins. Trypsin hydrolyzes amide bonds on the carboxyl sides of Lysine and Arginine, the basic amino acid residues. Chymotrypsin works at amide bonds that are on the carboxyl sides of all aromatic amino acids, such as phenylalanine, tyrosine, and tryptophan. Chymotrypsin also has a minor reaction with other nonpolar amino acids, such as leucine and isoleucine. Which holds true of Trypsin.
• More chemical reactions are catalyzed by trypsin.
• Trypsin is more specific in its action.
• Chymotrypsin is more specific in its action.
• More amino acids are catalyzed by Chymotrypsin.
Lipases are enzymes that catalyze the hydrolysis of ester bonds in triglycerides. With about the same effectiveness, these enzymes work on many different triglyceride structures such as the 2 triglycerides containing palmitic acid and oleic acid. What level of specificity is shown in this case?
• Linkage
• Group
• Stereochemical
• Absolute
Alcohol dehydrogenase is found primarily in the liver and stomach. It converts ethanol to acetaldehyde, a toxin which is then further broken down by acetaldehyde dehydrogenase to acetic acid, then to CO2 and H2O. What is the substrate of the alcohol dehydrogenase enzyme?
• acetaldehyde
• alcohol
• acetic acid
• ethanol
Enzyme and substrate make an analogy of the lock-and-key model. Together they unlock a/an ________.
• activation energy
• reactant
• chemical lock
• bond
Enzyme is used up in the chemical reaction which makes the enzyme visible in the product side of the chemical reaction.
• True
False
What ion channels open and propagate signals through the binding of their corresponding signaling molecule?
• Voltage-gated ion channels
• Mechanically-gated ion channels
• Ligand-gated ion channels
• Signal-gated ion channels
Why must acetylcholine and other neurotransmitters be degraded?
• to stop the monopoly of a neurotransmitter in binding to receptors.
• to prevent constant stimulation of the postsynaptic nerve cell
• to block the action of agonists that further activates receptors
• to prevent the depletion of neurotransmitters due to excessive firing
Enkephalins control the perception of pain. The drug Demerol relieves pain also by binding to the enkephalin receptors. What action is shown by Demerol?
• antagonist
• agonist
• competitive inhibition
• allosteric regulation
Caffeine enhances the action of cAMP by blocking the enzyme phosphodiesterase, which degrades cAMP. The enhancement of cAMP activity promotes the stimulatory action of caffeine known as _____.
• psychedelic
• depressant
• stimulant
• tranquilizer
The storage sites of acetylcholine neurotransmitters
• Postsynaptic vesicles
• Presynaptic vesicle
• Axon terminal membrane
• Nerve endings of axon terminal
The breakdown of acetylcholine yields
• acetate ion and choline.
• acetate and cholinesteras
• acetic acid and cholinesterate
• acetic acid and cholinergic acid
Two monoamine neurotransmitters, dopamine and serotonin, act by binding to what receptors?
• Adrenergic receptors
• Peptidergic receptors
• Cholinergic receptors
• Amino acid receptors
Two monoamine neurotransmitters are dopamine and serotonin. Which are their receptors?
• Peptidergic receptors
• Purinergic receptors
• Cholinergic receptors
• Adrenergic receptors
Cobratoxin causes paralysis by blocking the nerve receptor and interrupting the communication between the neuron and muscle cell. Which applies to Cobratoxin?
• agonist
• antagonist
• synergist
• protagonist
Which series of events describes the transmission of acetylcholine neurotransmitters?
• VI -> V -> I -> II -> IV -> III
• VI -> V -> II -> I -> IV -> III
• III -> V -> II -> I -> IV -> VI
• III -> V -> IV -> I -> II -> VI
A large number of hormones with steroid ring structures are hydrophobic. Hence, they can cross the plasma membranes of the cell through
• the receptors.
• diffusion.
• ion channels.
• carrier proteins.
Chemical messengers or hormones that can enter a cell and often act in the nucleus, where they alter the expression of specific genes.
• amino acid messengers
• steroid messengers
• adrenergic messengers
• cholinergic messengers
Alcohol dehydrogenase is found primarily in the liver and stomach. It converts ethanol to acetaldehyde, a toxin which is then further broken down by acetaldehyde dehydrogenase to acetic acid, then to CO2 and H2O. What is the substrate of the alcohol dehydrogenase enzyme?
• acetaldehyde
• alcohol
• acetic acid
• ethanol
Variations in receptor structure among cell types allow the same hormone to have different effects on different cells. The statement above refers to which cell in this illustration?
• Cell A
• Cell B
• Cell C
• Cell D
In the transmission of a nerve impulse or electrochemical signal, what triggers the ion channels of the next neuron to open?
The flow of the calcium ions to the end terminal
The binding of acetylcholine to the receptors
The release of the acetylcholine to the synaptic cleft
The flow of the potassium ions inside the neuron
Which amino acid is known to reduce neurotransmission?
• Lysine
• Threonine
• Glycine
• Glutamic acid
The location of most receptors in the cell for steroid hormones
• mitochondrion
• nucleus
• cell membrane
• cytoplasm
The following are known secondary messengers except ____.
• cyclic AMP (cAMP)
• Calcium ion (Ca2+)
• Inositol phosphate (IP3)
• Diacylglycerol (DAG)
• Carbonate (CO32-)
Which of these amino acids is a known excitatory neurotransmitter?
• Tyrosine
• Cysteine
• Asparagine
• Glutamine
Taurine, an inhibitory neurotransmitter, has an amino group. Why can it not be considered as amino acid found in proteins?
• It has a sulfonic acid group instead of a carboxylic acid.
• It has a sulfhydryl group instead of carboxyl group.
• Its functional groups are bonded to alpha carbon.
• Its functional groups do not include an amino group
The axon of neurons transmits an electrical signal through depolarization and repolarization of the membrane. What is synonymous with an electrical signal?
• Signaling molecule
• Neurotransmitter
• Voltage
• Ligand
A biomolecule like cAMP transmits the action of the chemical messenger to the inside of the cell, usually with amplification
• Primary messenger
• Secondary messenger
• Tertiary messenger
• General messenger
Through the action of ion channels, the entry of the sodium ions and exit of potassium ions across the membrane of the neuron is made possible. What type of transport is this?
• Simple diffusion
• Active transport
• Bulk transport
• Facilitated transport
Displayed is the nucleotide, the building block of Deoxyribonucleic acid (DNA). What group renders the acidity of DNA
A
B
C
D
The neurotransmitter dopamine is deficient in patients with Parkinson's disease. What type of messenger is dopamine?
• Cholinergic
• Peptidergic
• Monoamine
• Amino acid
Which of these statements holds true for the events involved in acetylcholine transmission?
• After a few milliseconds, acetylcholine is degraded and calcium ions (Ca+2) channels close.
• Sodium ions (Na+) have higher concentration outside the neuron so they enter the neuron.
• Potassium ions (K+) have higher concentration outside the neuron so they leave the neuron.
• A change of Na+ and Ca+2 concentrations is translated into a nerve signal.
Enkephalins are the first isolated brain peptides. Which amino acid marks the difference between Leucine enkephalin and Methionine enkephalin?
• 1st
• 2nd
• 5th
• 4 th
A protein molecule on the surface of the cell that recognizes and binds a neurotransmitter
• Ligand
• Receptor
• Active site
• Messenger
It is a membrane-bound enzyme that catalyzes the hydrolysis of GTP to GDP or GMP.
• GTP
• ATPase
• c-AMP
• G-protein
The receptors' binding sites for acetylcholine
• 5 AChR units
• 2 α subunits
• 2 β subunits
• 2 γ subunits
An enzyme kinase catalyzes the phosphorylation of Inositol-1,4-diphosphate to inositol-1,4,5- triphosphate. Which of these structural formulas is Inositol-1,4-diphosphate?
A
B
C
D
Which of the following is mismatched?
• Norepinephine - adrenergic messenger
• Thyroxine - amino acid messenger
• Oxytocin – amino acid messenger
• Acetylcholine – cholinergic messenger
The following hormones use the G-proteinadenylate cyclase cascade except _________.
• Glucagon
• Luteinizing hormone
• Antidiuretic hormone
• Epinephrine
The receptor subunit of insulin hormone that spans the cell membrane.
• α subunit
• β subunit
• γ subunit
• δ subunit
It causes the opening of ion channels and the entry of calcium ions into the nerve cell that leads to the release of neurotransmitter molecules into the synapse.
• Repolarization of the membrane of the neuron
• An electrical signal reaching the presynaptic site
• An electrochemical signal that gets the needed boost
• Signals from the postsynaptic site of the next neuron
They activate intracellular signaling pathways by amplifying the first communication signal and induce a cellular response.
• primary messengers
• secondary messengers
• electrochemical signals
• chemical messengers
These chemical messengers require a secondary messenger except
• adrenergic messengers.
• peptidergic messengers.
• cholinergic messengers.
• steroid messengers.
Hormone Endorphin has a similar structure to enkephalin. So it can bind to the receptor of enkephalin as well. What molecule is Endorphin given in this case?
• Antagonist
• Agonist
• Allosteric
• Competitive
What dose can make nicotine act as a stimulant that prolongs the receptor's biochemical response?
• large dose
• regular dose
• low dose
• excessive dose
Which molecule activates the protein kinase for it to dissociate the regulatory and catalytic subunits?
• Cyclic AMP
• G-protein
• GTP
• Adenylate cyclase
When 2 molecules of acetylcholine bind to the 2 AChR subunits, ion channel opens. What ions are allowed to pass through the open ion channel?
• Na+ and K+ ions
• Na+ and Ca+2 ions
• Ca+2 and K+ ions
• Mg+2 and K+ ions
