1Based on their shape, proteins are broadly classified into fibrous and which other type?
structural classification of proteins
Easy
A.Circular proteins
B.Helical proteins
C.Globular proteins
D.Linear proteins
Correct Answer: Globular proteins
Explanation:
Proteins are structurally classified as fibrous (elongated, structural) and globular (compact, functional) proteins.
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2Which of the following is an example of a fibrous protein?
structural classification of proteins
Easy
A.Hemoglobin
B.Collagen
C.Insulin
D.Myoglobin
Correct Answer: Collagen
Explanation:
Collagen is a fibrous structural protein, whereas hemoglobin, insulin, and myoglobin are globular proteins.
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3The three-dimensional arrangement of a single polypeptide chain is called its:
structural classification of proteins
Easy
A.Tertiary structure
B.Secondary structure
C.Quaternary structure
D.Primary structure
Correct Answer: Tertiary structure
Explanation:
Tertiary structure refers to the overall 3D folding of a single polypeptide chain, stabilized by various interactions.
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4Which level of protein structure refers to the linear sequence of amino acids?
structural classification of proteins
Easy
A.Primary structure
B.Quaternary structure
C.Secondary structure
D.Tertiary structure
Correct Answer: Primary structure
Explanation:
The primary structure is the specific linear sequence of amino acids linked by peptide bonds.
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5The -helix and -pleated sheet are examples of which level of protein structure?
structural classification of proteins
Easy
A.Primary structure
B.Tertiary structure
C.Secondary structure
D.Quaternary structure
Correct Answer: Secondary structure
Explanation:
The -helix and -pleated sheet are common secondary structures stabilized by hydrogen bonds.
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6Which protein is primarily responsible for oxygen transport in blood?
function of proteins
Easy
A.Keratin
B.Collagen
C.Hemoglobin
D.Actin
Correct Answer: Hemoglobin
Explanation:
Hemoglobin in red blood cells binds and transports oxygen throughout the body.
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7Which of the following is a defensive function performed by proteins?
function of proteins
Easy
A.Providing energy storage as fat
B.Storing genetic information
C.Antibodies fighting pathogens
D.Transmitting nerve impulses electrically
Correct Answer: Antibodies fighting pathogens
Explanation:
Antibodies (immunoglobulins) are proteins that defend the body by recognizing and neutralizing pathogens.
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8Which protein provides structural support and strength to skin, tendons, and bones?
function of proteins
Easy
A.Hemoglobin
B.Collagen
C.Insulin
D.Amylase
Correct Answer: Collagen
Explanation:
Collagen is a structural protein that provides strength and support to connective tissues.
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9Insulin is a protein that functions as a:
function of proteins
Easy
A.Transport channel
B.Enzyme
C.Hormone
D.Antibody
Correct Answer: Hormone
Explanation:
Insulin is a peptide hormone that regulates blood glucose levels.
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10A Ramachandran plot is used to display the allowed values of which two dihedral angles?
Ramachandran plot
Easy
A. (phi) and (psi)
B. and
C. and
D. and
Correct Answer: (phi) and (psi)
Explanation:
The Ramachandran plot maps the backbone dihedral angles and to show sterically allowed conformations.
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11The Ramachandran plot primarily helps identify which type of conformations for a polypeptide?
Ramachandran plot
Easy
A.Enzyme active sites
B.Amino acid sequences
C.Sterically allowed conformations
D.Denatured states only
Correct Answer: Sterically allowed conformations
Explanation:
The Ramachandran plot shows which combinations of backbone angles are sterically favorable or forbidden.
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12Which amino acid shows the greatest flexibility and occupies the widest region on a Ramachandran plot?
Ramachandran plot
Easy
A.Tryptophan
B.Glycine
C.Proline
D.Cysteine
Correct Answer: Glycine
Explanation:
Glycine has only a hydrogen as its side chain, allowing greater backbone flexibility and a wider allowed region.
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13Denaturation of a protein primarily results in the loss of its:
stability of proteins and denaturation
Easy
A.Three-dimensional structure
B.Amino acid composition
C.Primary sequence
D.Peptide bonds
Correct Answer: Three-dimensional structure
Explanation:
Denaturation disrupts the higher-order (secondary, tertiary, quaternary) structure without breaking peptide bonds.
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14Which of the following can cause denaturation of a protein?
stability of proteins and denaturation
Easy
A.Low salt concentration
B.Neutral pH
C.High temperature
D.Presence of water
Correct Answer: High temperature
Explanation:
High temperature disrupts the weak interactions stabilizing protein structure, causing denaturation.
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15Which type of bond remains intact during protein denaturation?
stability of proteins and denaturation
Easy
A.Hydrogen bonds
B.Peptide bonds
C.Hydrophobic interactions
D.Ionic bonds
Correct Answer: Peptide bonds
Explanation:
Denaturation disrupts weak stabilizing interactions but leaves the covalent peptide bonds of the primary structure intact.
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16According to the international classification, enzymes are divided into how many main classes?
classification of enzymes
Easy
A.Six
B.Eight
C.Three
D.Four
Correct Answer: Six
Explanation:
Enzymes are classified into six main classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
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17Enzymes that catalyze hydrolysis reactions belong to which class?
classification of enzymes
Easy
A.Ligases
B.Hydrolases
C.Oxidoreductases
D.Isomerases
Correct Answer: Hydrolases
Explanation:
Hydrolases catalyze the cleavage of bonds by adding water (hydrolysis).
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18In the Michaelis-Menten equation, represents the substrate concentration at which the reaction velocity is:
overview of enzyme kinetics
Easy
A.Half of
B.Zero
C.Equal to
D.Twice
Correct Answer: Half of
Explanation:
is the substrate concentration at which the reaction rate reaches half of the maximum velocity .
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19Most human enzymes show maximum activity at an optimum temperature of approximately:
factors affecting activity of enzymes
Easy
A.
B.
C.
D.
Correct Answer:
Explanation:
Human enzymes are most active around normal body temperature, .
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20Enzymes speed up reactions primarily by:
mechanism of enzyme catalysis
Easy
A.Changing the reaction equilibrium
B.Lowering the activation energy
C.Increasing the activation energy
D.Raising the temperature of the reaction
Correct Answer: Lowering the activation energy
Explanation:
Enzymes act as catalysts by lowering the activation energy required for a reaction to proceed, without altering equilibrium.
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21A protein is found to contain multiple polypeptide chains held together by non-covalent interactions, giving rise to a functional oligomer. Which level of protein structure does this arrangement represent?
structural classification of proteins
Medium
A.Secondary structure
B.Primary structure
C.Tertiary structure
D.Quaternary structure
Correct Answer: Quaternary structure
Explanation:
Quaternary structure describes the spatial arrangement of two or more polypeptide (subunit) chains held together mainly by non-covalent interactions to form a functional multi-subunit protein.
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22In an -helix, hydrogen bonds stabilizing the structure form between the C=O of one residue and the N–H group of which residue?
structural classification of proteins
Medium
A.The residue
B.The residue
C.The residue
D.The residue
Correct Answer: The residue
Explanation:
In an -helix, the carbonyl oxygen of residue hydrogen bonds to the amide hydrogen of residue , producing 3.6 residues per turn.
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23Keratin and collagen are commonly classified together based on their shape and solubility. Which category do they belong to?
structural classification of proteins
Medium
A.Conjugated proteins
B.Membrane proteins
C.Globular proteins
D.Fibrous proteins
Correct Answer: Fibrous proteins
Explanation:
Keratin and collagen are elongated, water-insoluble structural proteins, placing them in the fibrous protein category as opposed to compact, soluble globular proteins.
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24Hemoglobin transports oxygen in the blood. Which functional class of proteins best describes this role?
function of proteins
Medium
A.Storage proteins
B.Catalytic proteins
C.Transport proteins
D.Contractile proteins
Correct Answer: Transport proteins
Explanation:
Hemoglobin binds and carries oxygen through the circulation, a defining role of transport proteins. Enzymes are catalytic, actin/myosin are contractile, and ferritin is a storage protein.
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25A patient's immune response involves proteins that specifically recognize and bind foreign antigens. These proteins function primarily as:
function of proteins
Medium
A.Regulatory proteins
B.Defensive (immune) proteins
C.Structural proteins
D.Storage proteins
Correct Answer: Defensive (immune) proteins
Explanation:
Antibodies (immunoglobulins) recognize and bind antigens as part of the immune defense, classifying them functionally as defensive/protective proteins.
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26The Ramachandran plot displays the allowed conformations of a polypeptide backbone. Which two angles are plotted against each other?
Ramachandran plot
Medium
A. and
B. and
C. and
D. and
Correct Answer: and
Explanation:
The Ramachandran plot maps the backbone dihedral angles (about N–C) versus (about C–C), showing sterically allowed regions.
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27Which amino acid shows an unusually large allowed region in the Ramachandran plot due to the absence of a bulky side chain?
Ramachandran plot
Medium
A.Isoleucine
B.Glycine
C.Tryptophan
D.Proline
Correct Answer: Glycine
Explanation:
Glycine has only a hydrogen as its side chain, minimizing steric clashes and permitting a much wider range of / combinations than other residues.
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28In a Ramachandran plot, right-handed -helices and antiparallel -sheets appear in distinct clusters. Why are certain regions of the plot considered disallowed?
Ramachandran plot
Medium
A.Because hydrogen bonds cannot form there
B.Because of steric clashes between atoms
C.Because peptide bonds cannot rotate there
D.Because those angles break the peptide backbone
Correct Answer: Because of steric clashes between atoms
Explanation:
Disallowed regions correspond to / combinations that would force backbone or side-chain atoms into unacceptably close contact (steric overlap), making them energetically unfavorable.
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29During denaturation by heat, which of the following is typically disrupted while the primary structure remains intact?
stability of proteins and denaturation
Medium
A.Non-covalent interactions and folding
B.Peptide bonds
C.The genetic code
D.Amino acid sequence
Correct Answer: Non-covalent interactions and folding
Explanation:
Denaturation disrupts hydrogen bonds, ionic interactions, and hydrophobic packing that maintain higher-order structure, but the covalent peptide bonds of the primary sequence remain unbroken.
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30Urea and guanidinium chloride are commonly used to denature proteins. They act mainly by:
stability of proteins and denaturation
Medium
A.Disrupting the hydrophobic effect and hydrogen bonding
B.Cleaving peptide bonds
C.Adding phosphate groups
D.Oxidizing disulfide bonds
Correct Answer: Disrupting the hydrophobic effect and hydrogen bonding
Explanation:
Chaotropic agents like urea and guanidinium chloride interfere with hydrogen bonding and the hydrophobic interactions that stabilize folded proteins, causing unfolding without breaking peptide bonds.
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31Which type of covalent bond contributes to protein stability and can be reduced by agents such as -mercaptoethanol?
stability of proteins and denaturation
Medium
A.Disulfide bond
B.Phosphodiester bond
C.Peptide bond
D.Glycosidic bond
Correct Answer: Disulfide bond
Explanation:
Disulfide bonds between cysteine residues are covalent linkages that stabilize tertiary/quaternary structure; reducing agents like -mercaptoethanol break them to –SH groups.
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32An enzyme catalyzes the transfer of a phosphate group from ATP to glucose. According to the EC classification, this enzyme belongs to which class?
classification of enzymes
Medium
A.Hydrolases
B.Transferases
C.Oxidoreductases
D.Ligases
Correct Answer: Transferases
Explanation:
Transferases catalyze the transfer of functional groups (such as phosphate) between molecules; a kinase transferring phosphate from ATP is a transferase (EC 2).
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33Which enzyme class catalyzes the hydrolytic cleavage of bonds using water as a reactant?
classification of enzymes
Medium
A.Hydrolases
B.Lyases
C.Oxidoreductases
D.Isomerases
Correct Answer: Hydrolases
Explanation:
Hydrolases (EC 3) catalyze bond cleavage by the addition of water, e.g., proteases and lipases. Lyases cleave bonds without water, and isomerases rearrange within a molecule.
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34An enzyme converts glucose-6-phosphate to fructose-6-phosphate without changing the molecular formula. This reaction is catalyzed by an:
classification of enzymes
Medium
A.Ligase
B.Hydrolase
C.Isomerase
D.Oxidoreductase
Correct Answer: Isomerase
Explanation:
Interconversion of structural isomers such as glucose-6-phosphate and fructose-6-phosphate is catalyzed by isomerases (EC 5), which rearrange atoms within a single molecule.
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35For an enzyme obeying Michaelis–Menten kinetics, the is best described as the substrate concentration at which:
overview of enzyme kinetics
Medium
A.The enzyme is fully denatured
B.The reaction rate is half of
C.The reaction rate is maximal
D.All enzyme is free
Correct Answer: The reaction rate is half of
Explanation:
equals the substrate concentration at which the reaction velocity reaches half of , and it reflects the enzyme's apparent affinity for its substrate.
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36An enzyme has and . What is the reaction velocity when ?
overview of enzyme kinetics
Medium
A.
B.
C.
D.
Correct Answer:
Explanation:
When , the Michaelis–Menten equation gives .
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37In a Lineweaver–Burk (double reciprocal) plot, the y-intercept corresponds to:
overview of enzyme kinetics
Medium
A.
B.
C.
D.
Correct Answer:
Explanation:
The Lineweaver–Burk equation has a y-intercept of and x-intercept of .
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38Most enzymes show a bell-shaped curve of activity versus pH. This behavior is primarily because pH affects:
factors affecting activity of enzymes
Medium
A.The ionization of active-site residues
B.The number of enzyme molecules
C.The temperature of the reaction
D.The molecular weight of substrate
Correct Answer: The ionization of active-site residues
Explanation:
pH alters the protonation state of catalytic and binding residues (and substrate), so activity peaks at an optimal pH and declines on either side, giving a bell-shaped curve.
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39As temperature rises above an enzyme's optimum, reaction rate initially increases but then falls sharply. The decline is mainly due to:
factors affecting activity of enzymes
Medium
A.Reduced collision frequency
B.Decreased substrate concentration
C.Formation of more product
D.Thermal denaturation of the enzyme
Correct Answer: Thermal denaturation of the enzyme
Explanation:
Beyond the optimum temperature, the enzyme's three-dimensional structure unfolds (denatures), destroying the active site and causing a steep loss of catalytic activity.
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40The 'induced fit' model of enzyme catalysis differs from the 'lock and key' model because it proposes that:
mechanism of enzyme catalysis
Medium
A.The active site changes shape upon substrate binding
B.No conformational change ever occurs
C.The enzyme is consumed in the reaction
D.The substrate changes shape only
Correct Answer: The active site changes shape upon substrate binding
Explanation:
The induced fit model states that substrate binding induces a conformational change in the enzyme's active site, optimizing catalytic contacts, unlike the rigid lock-and-key view.
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41In a Ramachandran plot, glycine residues occupy a substantially larger allowed region than other amino acids. Which structural feature best explains this?
Ramachandran plot
Hard
A.Its side chain forms stabilizing hydrogen bonds that relax torsional limits
B.Its cyclic side chain restricts but frees rotation
C.Its bulky side chain forces residues into left-handed helical regions only
D.Absence of a side-chain atom minimizes steric clashes across and combinations
Correct Answer: Absence of a side-chain atom minimizes steric clashes across and combinations
Explanation:
Glycine's side chain is a single hydrogen atom, so it lacks the carbon that causes steric hindrance. This allows a much wider range of / angles, including regions forbidden for other residues.
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42Proline shows a highly restricted range of angles clustered near . What is the underlying reason?
Ramachandran plot
Hard
A.Its charged side chain electrostatically constrains rotation about -N
B.Its side chain covalently bonds back to the backbone nitrogen, locking the dihedral
C.Its aromatic ring sterically forces a single value
D.Its imino group forms an extra backbone hydrogen bond fixing
Correct Answer: Its side chain covalently bonds back to the backbone nitrogen, locking the dihedral
Explanation:
Proline's cyclic pyrrolidine ring links the side chain to the backbone amide nitrogen, physically constraining the N- bond and fixing near .
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43An enzyme has and . At a substrate concentration of , what is the reaction velocity?
overview of enzyme kinetics
Hard
A.
B.
C.
D.
Correct Answer:
Explanation:
When , the Michaelis-Menten equation gives , by definition of .
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44A competitive inhibitor is added to an enzyme reaction. On a Lineweaver-Burk plot, how do the intercepts change relative to the uninhibited reaction?
overview of enzyme kinetics
Hard
A.Both intercepts move toward the origin equally
B.Both intercepts increase proportionally
C.The -intercept is unchanged while the -intercept moves toward zero
D.The -intercept increases while the -intercept is unchanged
Correct Answer: The -intercept is unchanged while the -intercept moves toward zero
Explanation:
Competitive inhibition raises apparent but leaves unchanged. The -intercept () stays fixed, while the -intercept () moves toward zero as increases.
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45For an enzyme, and . What is the catalytic efficiency ?
overview of enzyme kinetics
Hard
A.
B.
C.
D.
Correct Answer:
Explanation:
. This value approaches the diffusion limit, indicating a highly efficient enzyme.
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46An enzyme shows maximal activity at pH 7. Activity drops sharply on both sides of this optimum. Which explanation is most consistent with this bell-shaped curve?
factors affecting activity of enzymes
Hard
A.A single ionizable group must be protonated for activity
B.Extreme pH values irreversibly hydrolyze all peptide bonds
C.Two ionizable catalytic groups must be in opposite protonation states for catalysis
D.The substrate binds only when fully deprotonated
Correct Answer: Two ionizable catalytic groups must be in opposite protonation states for catalysis
Explanation:
A bell-shaped pH-activity curve arises when two catalytic residues need specific, opposite protonation states. The rising limb reflects deprotonation of one group; the falling limb reflects protonation loss of the other.
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47In the serine protease chymotrypsin, which residues constitute the catalytic triad responsible for the nucleophilic attack?
mechanism of enzyme catalysis
Hard
A.Cys, His, Asn
B.Ser, His, Asp
C.Thr, His, Asp
D.Ser, Lys, Glu
Correct Answer: Ser, His, Asp
Explanation:
Chymotrypsin's catalytic triad is Ser-195, His-57, and Asp-102. Asp orients and polarizes His, which deprotonates Ser, generating a nucleophilic serine alkoxide that attacks the substrate carbonyl.
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48Transition-state analogs are often extremely potent enzyme inhibitors. What is the fundamental reason?
mechanism of enzyme catalysis
Hard
A.They form irreversible covalent bonds with the active site
B.They lower the activation energy of a competing reaction
C.Enzymes bind the transition state more tightly than substrate or product
D.They increase the entropy of the enzyme-substrate complex
Correct Answer: Enzymes bind the transition state more tightly than substrate or product
Explanation:
Catalysis works by stabilizing the transition state, so an enzyme's active site is complementary to it. Analogs resembling this state bind far more tightly than the substrate, making them potent inhibitors.
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49An enzyme catalyzes the transfer of a phosphate group from ATP to glucose. Under the EC classification system, which class does it belong to?
classification of enzymes
Hard
A.Transferases (EC 2)
B.Hydrolases (EC 3)
C.Ligases (EC 6)
D.Oxidoreductases (EC 1)
Correct Answer: Transferases (EC 2)
Explanation:
Hexokinase transfers a phosphoryl group from ATP to glucose. Group-transfer reactions are catalyzed by transferases (EC class 2); kinases are phosphotransferases within this class.
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50Which enzyme class specifically catalyzes the joining of two molecules coupled to the hydrolysis of a nucleoside triphosphate?
classification of enzymes
Hard
A.Hydrolases
B.Isomerases
C.Ligases
D.Lyases
Correct Answer: Ligases
Explanation:
Ligases (EC 6) join two substrates with formation of new C-O, C-S, C-N, or C-C bonds, coupled to cleavage of a triphosphate such as ATP. Lyases break bonds without hydrolysis or oxidation.
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51Which statement most accurately describes the thermodynamics of protein folding under physiological conditions?
stability of proteins and denaturation
Hard
A.Folding is driven entirely by enthalpy with negligible entropic contributions
B.The unfolded state is always enthalpically favored over the native state
C.The native state is stabilized by hundreds of of covalent energy
D.The native state is only marginally stable, with of unfolding around –
Correct Answer: The native state is only marginally stable, with of unfolding around –
Explanation:
Native proteins are marginally stable; the free energy difference between folded and unfolded states is small (roughly the energy of a few hydrogen bonds), allowing regulated folding and unfolding.
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52Urea and guanidinium chloride denature proteins primarily by which mechanism?
stability of proteins and denaturation
Hard
A.Cleaving disulfide bonds through reduction
B.Weakening the hydrophobic effect by increasing solubility of nonpolar groups
C.Chelating metal cofactors from the active site
D.Catalyzing hydrolysis of the peptide backbone
Correct Answer: Weakening the hydrophobic effect by increasing solubility of nonpolar groups
Explanation:
Chaotropic agents like urea and GdmCl disrupt the ordered water structure and increase solvation of nonpolar side chains, weakening the hydrophobic effect that stabilizes the folded core. They do not cleave covalent bonds.
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53In the classic hierarchy (SCOP/CATH), what distinguishes an protein from an protein?
structural classification of proteins
Hard
A. has interspersed, alternating helices and strands; has segregated all- and all- regions
B. lacks any -sheet; lacks any helix
C. contains only parallel sheets; contains only helices
D. is exclusively membrane-bound; is exclusively soluble
Correct Answer: has interspersed, alternating helices and strands; has segregated all- and all- regions
Explanation:
In proteins, -helices and -strands alternate along the chain (e.g., TIM barrels). In proteins, the helical and sheet segments are spatially segregated rather than interwoven.
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54A right-handed -helix has a rise of per residue and residues per turn. What is the pitch (rise per turn) of the helix?
structural classification of proteins
Hard
A.
B.
C.
D.
Correct Answer:
Explanation:
Pitch = rise per residue residues per turn . This is a defining geometric parameter of the standard -helix.
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55Hemoglobin exhibits a sigmoidal -binding curve while myoglobin is hyperbolic. The sigmoidal shape reflects which property?
function of proteins
Hard
A.Higher intrinsic affinity of a single binding site
B.Positive cooperativity among subunits due to allosteric conformational changes
C.Absence of any conformational change on ligand binding
D.Irreversible covalent binding of to iron
Correct Answer: Positive cooperativity among subunits due to allosteric conformational changes
Explanation:
Hemoglobin's four subunits interact allosterically; binding to one subunit increases affinity of the others (positive cooperativity), producing the sigmoidal curve. Monomeric myoglobin has no cooperativity, giving a hyperbolic curve.
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56For an enzyme obeying Michaelis-Menten kinetics, what fraction of is reached when ?
overview of enzyme kinetics
Hard
A.
B.
C.
D.
Correct Answer:
Explanation:
.
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57A noncompetitive inhibitor and a competitive inhibitor are compared. Which pair of effects on kinetic parameters is correct?
factors affecting activity of enzymes
Hard
A.Both leave and unchanged
B.Noncompetitive lowers with unchanged; competitive raises with unchanged
C.Noncompetitive raises ; competitive lowers
D.Both lower and raise equally
Correct Answer: Noncompetitive lowers with unchanged; competitive raises with unchanged
Explanation:
Classical noncompetitive inhibitors bind both E and ES, reducing without altering . Competitive inhibitors compete for the active site, increasing apparent while is unchanged at saturating substrate.
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58The proposed catalytic strategy in which an enzyme reduces the entropic cost of a reaction by binding substrates in the correct orientation is best described as:
mechanism of enzyme catalysis
Hard
A.Proximity and orientation effects
B.Covalent catalysis
C.General acid-base catalysis
D.Metal-ion catalysis
Correct Answer: Proximity and orientation effects
Explanation:
By binding and precisely aligning substrates, enzymes reduce the loss of translational and rotational entropy required to reach the transition state, accelerating the reaction. This is distinct from acid-base, covalent, or metal-ion mechanisms.
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59Anfinsen's ribonuclease refolding experiment demonstrated which principle?
stability of proteins and denaturation
Hard
A.Chaperones are always required for correct disulfide formation
B.Denaturation is invariably irreversible for globular proteins
C.The primary sequence contains all information needed to specify the native 3D structure
D.Native structure is determined solely by the cell's redox potential
Correct Answer: The primary sequence contains all information needed to specify the native 3D structure
Explanation:
Anfinsen showed denatured, reduced RNase A could spontaneously refold to its active native form once denaturant and reductant were removed, proving that the amino acid sequence dictates the folded structure.
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60The binding of 2,3-bisphosphoglycerate (2,3-BPG) to hemoglobin has what functional consequence?
function of proteins
Hard
A.It stabilizes the T (deoxy) state, lowering affinity and promoting release to tissues
B.It converts hemoglobin into a monomeric, non-cooperative form
C.It stabilizes the R state, increasing affinity in the lungs
D.It covalently modifies the heme iron to block binding
Correct Answer: It stabilizes the T (deoxy) state, lowering affinity and promoting release to tissues
Explanation:
2,3-BPG binds in the central cavity of deoxyhemoglobin, stabilizing the low-affinity T state. This shifts the dissociation curve rightward, enhancing oxygen unloading in peripheral tissues.
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