Biology practice questions & answers Flashcards
Mendelian genetic
_ If the phenotype skips 1 generation, then it is recessive
_ Mother to son transmission is the hallmark of X-linked disorder
Autosomal inheritance
In autosomal inheritance, each offspring receives one allele from the father and one from the mother.
Autosomal recessive inheritance
In an autosomal recessive disorder, the offspring has to receive two disease alleles to exhibit the disease phenotype.
A carrier of an autosomal recessive disorder possesses one diseased allele and one normal allele.
What charge does amino acids with acidic side have at physiologic pH ~7.4
Amino acids with acidic side groups carry a net negative charge at physiologic pH.
A polypeptide with a net positive charge at physiologic pH (~7.4) most likely contains amino acids with R groups of what type?
Basic R group
The amino acids in hemoglobin (or any protein) uniformly have which of the following configurations?
All biologically produced amino acids are in the L configuration.
Which of the following properties of a protein is least likely to be affected by changes in pH?
Primary structure is the amino acid sequence of a protein plus the peptide bonds joining them together.
Change in pH are unlikely to alter amino acid sequence or break peptide bonds.
The primary structure of a protein is least likely to be affected by changes in pH.
Hydrogen bonding between separate subunits of DNA polymerase is an example of which of the following?
1 degree structure through 3 degree structure have to do with individual polypeptides.
Hint #2
4 degree structure refers to the global three dimensional arrangements found in multi-subunit proteins.
Hint #3
Hydrogen bonding between separate subunits of DNA polymerase is an example of 4 degree structure.
The unique cyclic structure of which of the following amino acids plays a central role in the formation of alpha helices and beta sheets?
Please choose from one of the following options.
Lysine
Arginine
Valine
Proline
Alpha helices and beta sheets are two three dimensional motifs that regularly appear in local segments of amino acids.
Hint #2
Proline has a unique cyclic structure which differentiates it from the other common amino acids.
Hint #3
Proline plays a central role in the FORMATION of alpha helices and beta sheets. While proline’s unique structure may also disrupt both alpha helixes and beta sheets, it’s ability to make sharp turns facilitates the FORMATION of both structures, with proline commonly being found at the beginning of alpha helices or at the turns in beta sheets.
Electrophoretic separation of leucine from a protein sample would be least effective at which of the following pH values?
Please choose from one of the following options.
2.4
1.4
0.4
7.4
Leucine has an aliphatic side chain.
Hint #2
At physiological pH, leucine exists as a zwitterion.
Hint #3
Electrophoretic separation of leucine from a protein sample would be least effective at pH 7.4.
Electrophoretic separation at pH 6 of a sample of polypeptide 1 (mw 100) polypeptide 2 (mw 200) and polypeptide 3 (mw 400) would result in which of the following?
(Note: the isoelectric point of each polypeptide occurs at pH 6)
Please choose from one of the following options.
Polypeptide 3 would move the farthest
Polypeptide 1 would move the farthest
Polypeptide 2 would move the farthest
None of the polypeptides would move
The isoelectric point for a polypeptide is the pH at which the molecule does not have a net charge.
Hint #2
Electrophoretic separation depends on the existence of a negative net charge.
Hint #3
None of the polypeptides would move at pH 6.
Phosphoglucomutase, which catalyses the formation of glucose-6-phosphate from glucose-1-phosphate, is best classified as which of the following enzyme type?
Please choose from one of the following options.
Kinase
Oxidoreductase
Isomerase
Lyase
Enzymes are classified according to the sort of reaction they catalyze.
Hint #2
glucose-6-phosphate is an isomer of glucose-1-phosphate.
Hint #3
Phosphoglucomutase is an isomerase.
Which of the following molecules cannot be classified as an enzymatic cofactor?
Please choose from one of the following options.
Heme
Valine
Mg2+
Flavin adenine dinucleotide (FAD)
A cofactor is a nonorganic molecule whose presence is necessary for the proper function of an enzyme.
Hint #2
Valine is an organic molecule, namely an amino acid.
Hint #3
Valine cannot be classified as an enzymatic cofactor.
In order to analyze the catalytic effect of two different enzymes on the same chemical reaction, it is best to compare which of the following quantities?
Please choose from one of the following options.
The differences in enthalpy between the reactants and products
The differences in entropy between the reactants and products
The differences in free energy between the reactants and products
The difference between transition state energies
Analyzing the catalytic effect of two different enzymes on a chemical reaction requires comparison between the reaction kinetics.
Hint #2
Entropy, enthalpy, and free energy are all thermodynamic quantities.
Hint #3
In order to analyze the catalytic effect of two different enzymes on the same chemical reaction, it is best to compare differences in transition state energies.
The active site of an enzyme E, which catalyzes a reaction X, is partially denatured: which of the following quantities associated with X is most likely to be affected by the partial denaturation of E compared to the native form of E? Please choose from one of the following options. the equilibrium constant Keq the boltzmann constant kB the heat of reaction ΔH the rate-constant k
Denaturation of an enzyme will alter the kinetics of a reaction that it catalyzes.
Hint #2
The kinetics of a reaction can be characterized by a rate-constant.
Hint #3
Denaturation of E is most likely to affect the rate-constant associated with X.
The induced fit model of enzyme binding states that which of the following molecules alters the enzyme active site to more closely match the shape of the substrate?
Please choose from one of the following options.
A cofactor
A coenzyme
An allosteric effector
The substrate
A substrate for an enzyme is the reactant of the reaction that the enzyme catalyzes.
Hint #2
An enzyme and a substrate must come into close physical proximity for binding to occur, and such proximity can introduce physical forces that alter the shape of the enzyme.
Hint #3
The induced fit model of enzyme binding states that the substrate itself alters the enzyme active site.
Which of the following enzyme types catalyzes the formation of a single bond between two substrates through the elimination of H2O
Please choose from one of the following options.
Ligase
Oxidoreductase
Isomerase
Hydrolase
Classes of enzymes are named after the sort of reaction that they catalyze.
Hint #2
A ligase catalyzes the “ligation” of two molecules via the formation of a covalent bond.
Hint #3
A hydrolase catalyzes a reaction opposite to the sort catalyzed by a ligase: the hydrolysis of a covalent bond.
Local conditions can affect the specificity of an enzyme for its substrate, and thus the enzymes catalytic ability: which of the following alterations would most likely not affect an enzyme in this manner?
Please choose from one of the following options.
Increased temperature
Increased substrate concentration
Increased concentration of H+
Increased concentration of OH-
The specificity of an enzyme for its substrate is partially governed by the shape of the enzyme active site.
Hint #2
An enzyme active site is stabilized by non-covalent intramolecular interactions.
Hint #3
Non-covalent intramolecular interactions are affected by heat and pH, amongst other things.
Hint #4
Alterations in substrate concentration would not affect the specificity of an enzyme for its substrate.
Given that ∆G’° for the reaction S⇋P is negative in the direction of S→P, reaction equilibrium favors the formation of which substance?
Please choose from one of the following options.
S
The reaction does not proceed in either direction
The reaction proceeds equally in both directions
P
A negative standard free energy change (∆G’°) indicates the free energy of the ground state product formed from the reaction (P) is lower than that of S.
Hint #2
The negative standard free energy change of this reaction suggests that energy is released as S is converted to P.
Hint #3
The reverse reaction, therefore, would require energy to form S from P.
Hint #4
Reactions proceed spontaneously in the direction of the formation of low energy products from high energy reactants.
Hint #5
Given that ∆G’° for the reaction S⇋P is negative in the direction of S→P, reaction equilibrium favors the formation of P.
How would the addition of a catalyst to the reaction S⇋P affect the difference between the free energies of S and P in their ground states (∆G’°)?
Please choose from one of the following options.
The change in ∆G’° cannot be predicted without more information
∆G’° would become less negative
∆G’° would not change
∆G’° would become more negative
A catalyst functions by lowering the activation energy required for a reaction to proceed.
Hint #2
The overall energy change from the beginning to the end of a reaction is not affected by the addition of a catalyst.
Hint #3
A catalyst affects reaction rate, but does not alter the position or direction of equilibrium.
Hint #4
The addition of a catalyst to the reaction S⇋P would not affect the difference between the free energies of S and P in their ground states, therefore ∆G’° would not change.
For the enzyme-catalyzed reaction E + S ⇋ ES ⇋ E + P, what equation defines the rate at which ES is formed? ([Et ]= total enzyme concentration, [ES]= enzyme-substrate complex concentration, [S]=substrate concentration, [P]= product concentration, k1
=rate constant for ES formation from E and S, k-1 = reverse reaction rate constant)
Please choose from one of the following options.
k1[S]
k-1S
k1([Et]-[ES])[S]
k-1[S]
The rate of a reaction is dependant upon the concentration of reactants.
Hint #2
The rate of the reaction is equal to the rate constant times the concentration of reactants.
Hint #3
As ES is formed, the amount of unbound E and S decreases.
Hint #4
[Et] - [ES] is equal to the concentration of unbound enzyme, [E].
Hint #5
The rate at which ES is formed is k1([Et]-[ES])[S]
Problem
If the enzyme-catalyzed reaction E + S ⇋ ES ⇋ E + P is proceeding at or near the V{max} of E, what can be deduced about the relative concentrations of S and ES?
Please choose from one of the following options.
[S] is vanishingly low, [ES] is vanishingly low
S is abundant, [ES] is at its highest point
S is abundant, [ES] is vanishingly low
[S] is vanishingly low, [ES] is at its highest point
At V_{max}
max, the reaction is proceeding at a rate which is equal to the physiologic rate at which the enzyme can function.
Hint #2
At V_{max}, the enzyme is fully saturated, and no more free enzyme is available to bind the substrate and catalyze the reaction.
Hint #3
If all of the enzyme, E, is bound and operating, it must all exist in the ES state.
Hint #4
In order to maintain V_{max}
max, there must be sufficient substrate for the enzyme to bind, so [S] must be high enough to sustain this saturated state.