Struggling To Pass Biochemistry In Midterm? This Quiz Is The Key
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Biochemistry is the application of chemistry to the study of biological processes at the cellular and molecular level. It emerged as a distinct discipline around the beginning of the 20th century when scientists combined chemistry, physiology, and biology to investigate the chemistry of living systems.
Struggling To Pass BioChemistry In Midterm? This Quiz Is The Key
Questions and Answers
- 1.
What properties unite H, C, N, and O to make them appropriate to form 99% of atoms in the human body?
- 2.
Describe and differentiate between the four classes of macromolecules.
- 3.
What is the primary difference between plant and animal cells?
- 4.
How do buffers work?
- 5.
What does the Henderson Hasselbach equation measure?
- 6.
What does the Gibbs Free Energy equation measure?
- 7.
Describe the process of determining an amino acid sequence
- 8.
List and describe why the structural properties of water and solvent properties of water are important?
- 9.
What makes carbon such an abundant element in biomolecules?
- A.
It can form up to five bonds by sharing its electrons.
- B.
It forms only single bonds.
- C.
It provides low bond energy.
- D.
It forms stable covalent bonds by electron pair sharing.
- E.
It does not usually bond to other carbons, allowing a more diverse combination of elements.
Correct Answer
D. It forms stable covalent bonds by electron pair sharing.Explanation
Carbon is an abundant element in biomolecules because it can form stable covalent bonds by sharing its electrons. This allows carbon to easily bond with other elements, creating a wide variety of complex molecules necessary for life. Carbon's ability to form multiple bonds also contributes to its versatility in forming different biomolecules, as it can form up to five bonds. Additionally, carbon's ability to form stable covalent bonds provides structural stability to biomolecules, ensuring their functionality.Rate this question:
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- 10.
The structural integrity of supramolecular complexes (assemblies) of multiple components are bonded to each other by all of the following forces EXCEPT:
- A.
Covalent bonds
- B.
van der Waals forces
- C.
hydrogen bonds
- D.
Hydrophobic interactions
- E.
Ionic interactions
Correct Answer
A. Covalent bondsExplanation
Supramolecular complexes are held together by various intermolecular forces such as van der Waals forces, hydrogen bonds, hydrophobic interactions, and ionic interactions. However, covalent bonds are not involved in the bonding of supramolecular complexes. Covalent bonds involve the sharing of electrons between atoms, leading to a strong and permanent bond. In contrast, supramolecular complexes are formed through weaker, non-covalent interactions that can be reversible and dynamic. Therefore, the correct answer is covalent bonds.Rate this question:
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- 11.
By limiting the orientation that neighboring water molecules can assume, solutes give ____ to the solvent and ____ the dynamic interplay among H2O molecules that occurs in pure water.
- A.
Pressure, disrupt
- B.
Disorder, increase
- C.
disorder, decrease
- D.
Order, diminish
- E.
Order, increase
Correct Answer
D. Order, diminishExplanation
Solute molecules restrict the possible orientations of neighboring water molecules, leading to a decrease in disorder and an increase in order in the solvent. This disruption of the dynamic interplay among water molecules reduces the overall level of disorder and diminishes the randomness in the system.Rate this question:
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- 12.
Buffer systems are effective when the pH values are within ____ pH unit(s) of the pKa value.
- A.
1
- B.
2
- C.
3
- D.
4
- E.
5
Correct Answer
A. 1Explanation
Buffer systems are effective when the pH values are within 1 pH unit of the pKa value. This is because the pKa value represents the point at which the concentration of the acid and its conjugate base are equal. When the pH is within 1 unit of the pKa, the buffer system can effectively resist changes in pH by accepting or donating protons to maintain a relatively constant pH.Rate this question:
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- 13.
To predict whether pairs of coupled reactions will proceed spontaneously:
- A.
Subtract the smaller from the larger ΔG.
- B.
Sum the ΔG°′ values for each reaction.
- C.
Add the ΔS values for each reaction at constant temperature.
- D.
The absolute value of the positive ΔG°′ must be larger than the value of the negative ΔG°′.
- E.
None are true.
Correct Answer
B. Sum the ΔG°′ values for each reaction.Explanation
The explanation for the given correct answer is that in order to predict whether pairs of coupled reactions will proceed spontaneously, we need to sum the ΔG°' values for each reaction. This is because the ΔG°' value represents the change in free energy under standard conditions, and by summing these values, we can determine the overall change in free energy for the coupled reactions. If the sum of the ΔG°' values is negative, it indicates that the reaction will proceed spontaneously.Rate this question:
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- 14.
Enthalpy change, ΔH, is:
- A.
The sum of heat absorbed and work.
- B.
Not a thermodynamic state function.
- C.
A measure of disorder in a system.
- D.
Determined by pressure change at a constant temperature.
- E.
Equal to the heat transferred at constant pressure and volume.
Correct Answer
E. Equal to the heat transferred at constant pressure and volume.Explanation
Enthalpy change, ΔH, is equal to the heat transferred at constant pressure and volume. This is because enthalpy is defined as the heat content of a system at constant pressure, and it includes both the heat absorbed or released by the system and the work done by or on the system. Therefore, the correct answer is that ΔH is equal to the heat transferred at constant pressure and volume.Rate this question:
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- 15.
The amino and carboxyl groups of amino acids react in a head-to-tail fashion, eliminating water, and forming a covalent ____ linkage typically referred to as a(n) ____ bond.
- A.
Ester, aromatic
- B.
Anhydride, phosphoanhydride
- C.
Amide, peptide
- D.
Dehydration, hydrogen
- E.
None of the above
Correct Answer
C. Amide, peptideExplanation
The amino and carboxyl groups of amino acids react in a head-to-tail fashion, eliminating water, and forming a covalent amide linkage typically referred to as a peptide bond.Rate this question:
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- 16.
The peptide bond has partial ____ character.
- A.
Hydrogen bond
- B.
Double bond
- C.
Triple bond
- D.
Van der Waals forces
- E.
All of the above
Correct Answer
B. Double bondExplanation
The peptide bond has partial double bond character because it exhibits characteristics of both a single bond and a double bond. This is due to the resonance structure of the peptide bond, where the electrons are delocalized between the carbon, nitrogen, and oxygen atoms. This delocalization results in a shorter bond length and greater bond strength, similar to a double bond.Rate this question:
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- 17.
A common reaction of two cysteine residues in proteins results in the formation of ____.
- A.
Thioester bonds
- B.
Disulfide bonds
- C.
Dithiol bonds
- D.
Thioether bonds
- E.
None of the above
Correct Answer
B. Disulfide bondsExplanation
When two cysteine residues in proteins react, they form disulfide bonds. Disulfide bonds are covalent bonds that connect two sulfur atoms in cysteine residues. These bonds play a crucial role in stabilizing the three-dimensional structure of proteins by forming bridges between different parts of the protein chain. They can also be involved in protein folding, regulation of protein activity, and protein-protein interactions. Thioester bonds involve the reaction of a carboxylic acid with a thiol, while dithiol bonds involve the reaction of two thiol groups. Thioether bonds involve the reaction of a sulfur atom with a carbon atom.Rate this question:
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- 18.
α-Helix and β-strand are components of ____ structure
- A.
Primary
- B.
Secondary
- C.
Tertiary
- D.
Quaternary
- E.
All are true
Correct Answer
B. SecondaryExplanation
α-Helix and β-strand are components of secondary structure. Secondary structure refers to the local folding patterns within a protein, specifically the regular repeating patterns of hydrogen bonding between the backbone atoms. The α-helix is a right-handed coil formed by a polypeptide chain, while the β-strand is a fully extended, zigzag conformation. These secondary structures are important for stabilizing the overall protein structure and are commonly observed in proteins. The primary structure refers to the linear sequence of amino acids, while tertiary and quaternary structures involve the overall three-dimensional folding and assembly of the protein, respectively.Rate this question:
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- 19.
Electrostatic interactions among amino acid residues on proteins may be damped out by high concentrations of:
- A.
Water
- B.
Organic solvents
- C.
Salts
- D.
Heat
- E.
All of the above
Correct Answer
C. SaltsExplanation
High concentrations of salts can dampen electrostatic interactions among amino acid residues on proteins. Salts, such as sodium chloride, contain ions that can disrupt the charges on the amino acid residues, reducing the strength of the electrostatic interactions. This is because the ions in the salt solution can compete with the amino acid residues for binding to each other, effectively neutralizing the charges and weakening the electrostatic interactions. Therefore, the correct answer is salts.Rate this question:
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- 20.
____ are proteins that help other proteins to fold.
- A.
Immunoglobins
- B.
Phospholipases
- C.
Synthetases
- D.
Molecular chaperones
- E.
Proteases
Correct Answer
D. Molecular chaperonesExplanation
Molecular chaperones are proteins that assist in the folding of other proteins. They help newly synthesized proteins to fold correctly into their functional three-dimensional structures. Molecular chaperones prevent misfolding, aggregation, and degradation of proteins, ensuring their proper folding and stability. They also aid in the refolding of denatured proteins under stress conditions. Therefore, molecular chaperones play a crucial role in maintaining protein homeostasis and preventing the formation of protein aggregates, which can lead to various diseases.Rate this question:
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- 21.
What are the most common elements that can form 99% of the biomolecules in humans?
Correct Answer
H, C, N, OExplanation
The most common elements that can form 99% of the biomolecules in humans are hydrogen (H), carbon (C), nitrogen (N), and oxygen (O). These elements are essential components of carbohydrates, lipids, proteins, and nucleic acids, which are the building blocks of life. Hydrogen and oxygen are present in water molecules, while carbon and nitrogen are found in organic compounds. Together, these elements make up a large majority of the biomolecules that are vital for the functioning of the human body.Rate this question:
- 22.
T/F? The correct structural organization of complex molecules is: inorganic precursor -> metabolite -> building blocks -> macromolecules
- A.
True
- B.
False
Correct Answer
A. TrueExplanation
The correct structural organization of complex molecules follows a specific order. It starts with inorganic precursors, which are transformed into metabolites. Metabolites then serve as building blocks for the formation of macromolecules. This sequence ensures that complex molecules are formed in a step-by-step manner, with each stage building upon the previous one. Therefore, the given statement that the correct structural organization of complex molecules is "inorganic precursor -> metabolite -> building blocks -> macromolecules" is true.Rate this question:
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- 23.
What two energy rich molecules react to provide us energy?
Correct Answer
ATP and NADPHExplanation
ATP (adenosine triphosphate) and NADPH (nicotinamide adenine dinucleotide phosphate) are both energy-rich molecules that play crucial roles in cellular energy metabolism. ATP is often referred to as the "energy currency" of the cell, as it stores and transfers energy within cells for various processes. NADPH, on the other hand, is involved in redox reactions and acts as a reducing agent, providing electrons for various metabolic reactions. Together, ATP and NADPH participate in cellular respiration and photosynthesis, respectively, to provide us with energy.Rate this question:
- 24.
Biomolecular recognition is mediated by _____________
Correct Answer
weak chemical forcesExplanation
Biomolecular recognition refers to the specific binding between biomolecules, such as proteins and DNA. This recognition is mediated by weak chemical forces, such as hydrogen bonding, van der Waals forces, and hydrophobic interactions. These forces are not as strong as covalent bonds but are essential for the formation and stability of biomolecular complexes. Weak chemical forces allow biomolecules to interact selectively and reversibly, enabling various biological processes such as enzyme-substrate interactions, protein-protein interactions, and DNA-protein binding.Rate this question:
- 25.
Molecules that interact with both polar and non-polar environments. They have hydrophilic and hydrophobic PROPERTIES
- A.
Amphiphilic
- B.
Amphipathic
Correct Answer
A. AmpHipHilicExplanation
Amphiphilic molecules have both hydrophilic and hydrophobic properties, allowing them to interact with both polar and non-polar environments. This means that they can dissolve in both water (a polar solvent) and oil (a non-polar solvent). The term "amphiphilic" describes the dual nature of these molecules, as they possess both hydrophilic (water-loving) and hydrophobic (water-repelling) regions. This property is essential for various biological processes, such as the formation of cell membranes, where the hydrophilic head groups interact with water while the hydrophobic tail regions interact with lipids.Rate this question:
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- 26.
Molecules that contain both polar and non-polar groups. These molecules have both hydrophilic and hydrophobic GROUPS in their composition
- A.
Amphipathic
- B.
Amphiphilic
Correct Answer
A. AmpHipathicExplanation
Amphipathic molecules are those that contain both polar and non-polar groups. This means that they have both hydrophilic (water-loving) and hydrophobic (water-fearing) groups in their composition. The presence of both types of groups allows these molecules to interact with both polar and non-polar substances, making them essential in various biological processes such as cell membrane formation and the transport of lipids and proteins. Amphipathic molecules can arrange themselves in unique ways, forming structures like micelles or lipid bilayers, which enable them to effectively interact with their surroundings.Rate this question:
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- 27.
This term for 3D structure describes a change from L-state to D-state by bond breakage and formation
- A.
Configuration
- B.
Conformation
Correct Answer
A. ConfigurationExplanation
The term "configuration" refers to the arrangement of atoms in a molecule. In this context, the change from L-state to D-state suggests a change in the spatial arrangement of the molecule due to bond breakage and formation. This change could result in a different configuration of the molecule, indicating a change in its 3D structure. Therefore, "configuration" is the correct answer.Rate this question:
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- 28.
This term for 3D structure describes the rotation of a molecule without bond breakage. This means it occurs through freely rotating single bonds.
- A.
Conformation
- B.
Configuration
Correct Answer
A. ConformationExplanation
Conformation refers to the different spatial arrangements or shapes that a molecule can adopt through the rotation of its single bonds without breaking them. It is important to note that conformational changes do not involve any bond breakage, only the rotation of single bonds. This term is used to describe the various 3D structures that a molecule can assume, which can have implications for its physical and chemical properties. Configuration, on the other hand, refers to the spatial arrangement of atoms in a molecule that cannot be interconverted without breaking covalent bonds.Rate this question:
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- 29.
This group is important to the function of the non-amino acid part of a protein:
Correct Answer
prosthetic groupExplanation
A prosthetic group is a non-amino acid molecule that is tightly bound to a protein and is essential for its function. It can be a metal ion, a coenzyme, or a lipid. Prosthetic groups play a crucial role in the catalytic activity or structural stability of proteins. They can participate in electron transfer reactions, act as cofactors, or help in binding substrates. Therefore, this group is important for the proper functioning of the non-amino acid part of a protein.Rate this question:
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Mar 21, 2023Quiz Edited by
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Jun 03, 2021Quiz Created by
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