Podcast
Questions and Answers
What is the result of differing electronegativities in a molecule?
What is the result of differing electronegativities in a molecule?
- A complete transfer of electrons
- The formation of an electric dipole (correct)
- The creation of a triple bond
- The breaking of a covalent bond
What is the approximate percentage of oxygen in a human being?
What is the approximate percentage of oxygen in a human being?
- 96% (correct)
- 70%
- 90%
- 80%
What is the primary reason for the formation of hydrogen bonds between water molecules?
What is the primary reason for the formation of hydrogen bonds between water molecules?
- The similarities in electronegativities between oxygen and hydrogen atoms
- The differences in electronegativities between oxygen and hydrogen atoms (correct)
- The ability of water to dissolve other polar compounds
- The presence of a double bond between oxygen and hydrogen atoms
What is the approximate energy required to break a hydrogen bond?
What is the approximate energy required to break a hydrogen bond?
What is the common trait shared by all living organisms on Earth?
What is the common trait shared by all living organisms on Earth?
How many major types of biomolecules are found in living organisms?
How many major types of biomolecules are found in living organisms?
Which of the following functional groups does not form hydrogen bonds?
Which of the following functional groups does not form hydrogen bonds?
What is the number of different amino acids found in biological molecules?
What is the number of different amino acids found in biological molecules?
Why do polar compounds dissolve in water?
Why do polar compounds dissolve in water?
What is the variable part of an amino acid?
What is the variable part of an amino acid?
What is the term for the electrostatic connections between water molecules?
What is the term for the electrostatic connections between water molecules?
What is the result of amino acids polymerizing to form proteins?
What is the result of amino acids polymerizing to form proteins?
What type of interactions are important in biochemistry?
What type of interactions are important in biochemistry?
What is the significance of the shape of a protein?
What is the significance of the shape of a protein?
What is the term for the bonding between water and other functional groups?
What is the term for the bonding between water and other functional groups?
What is the name of the force that brings hydrophobic residues together?
What is the name of the force that brings hydrophobic residues together?
What is the term for the shorter sequence of amino acids that make up a protein?
What is the term for the shorter sequence of amino acids that make up a protein?
What is the pH of a solution in which the concentration of H+ is equal to the concentration of OH-?
What is the pH of a solution in which the concentration of H+ is equal to the concentration of OH-?
What type of biomolecule is Met-Enkephalin?
What type of biomolecule is Met-Enkephalin?
What is the name of the equation that describes the extent of ionization of water?
What is the name of the equation that describes the extent of ionization of water?
What is the term for the hydrophobic groups in a protein structure?
What is the term for the hydrophobic groups in a protein structure?
What type of bonds are responsible for the stability of protein 3D structure?
What type of bonds are responsible for the stability of protein 3D structure?
What is the name of the protein that illustrates the principles of tertiary structure?
What is the name of the protein that illustrates the principles of tertiary structure?
What is the role of proline residues in protein structure?
What is the role of proline residues in protein structure?
What is the term used to describe the clustering of hydrophobic residues in protein structure?
What is the term used to describe the clustering of hydrophobic residues in protein structure?
What is the term used to describe the process of protein folding into a compact structure?
What is the term used to describe the process of protein folding into a compact structure?
What is a characteristic of proteins that are highly stable?
What is a characteristic of proteins that are highly stable?
What is the result of hydrophobic collapse and formation of secondary structures?
What is the result of hydrophobic collapse and formation of secondary structures?
What limits the amount of motion a protein can undergo and the number of conformations it can achieve?
What limits the amount of motion a protein can undergo and the number of conformations it can achieve?
What is the process of protein folding?
What is the process of protein folding?
What is the result of the series of smaller changes involving fewer residues?
What is the result of the series of smaller changes involving fewer residues?
What is the role of hydrophobic collapse in protein folding?
What is the role of hydrophobic collapse in protein folding?
What is true about the free-energy funnel of protein folding?
What is true about the free-energy funnel of protein folding?
What is the relationship between the number of amino acids and the formation of 3D structure?
What is the relationship between the number of amino acids and the formation of 3D structure?
What is the primary function of chaperone proteins in protein folding?
What is the primary function of chaperone proteins in protein folding?
What happens to the shape of a chaperone protein when it binds ATP?
What happens to the shape of a chaperone protein when it binds ATP?
What is the result of protein misfolding?
What is the result of protein misfolding?
What is the native structure of a protein?
What is the native structure of a protein?
What is the role of heat shock proteins in protein folding?
What is the role of heat shock proteins in protein folding?
What is the result of chaperone proteins releasing misfolded proteins?
What is the result of chaperone proteins releasing misfolded proteins?
What is the characteristic of a protein surface recognized by chaperone proteins?
What is the characteristic of a protein surface recognized by chaperone proteins?
What are diseases resulting from the formation of protein aggregates called?
What are diseases resulting from the formation of protein aggregates called?
Flashcards
Elements in the Human Body
Elements in the Human Body
The human body is primarily composed of 96% hydrogen, carbon, nitrogen, and oxygen.
Four Major Biomolecules
Four Major Biomolecules
The four major types are amino acids, carbohydrates, lipids, and nucleic acids.
Amino Acids
Amino Acids
Amino acids are the building blocks of proteins with a central carbon atom and unique R groups.
R Group of Amino Acids
R Group of Amino Acids
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Polymerization of Amino Acids
Polymerization of Amino Acids
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Primary Structure of Proteins
Primary Structure of Proteins
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Secondary Structure of Proteins
Secondary Structure of Proteins
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Role of Hydrophobic R Groups
Role of Hydrophobic R Groups
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Protein Function and Structure
Protein Function and Structure
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Hydrogen Bonds
Hydrogen Bonds
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Breaking Hydrogen Bonds
Breaking Hydrogen Bonds
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Importance of pH
Importance of pH
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Keq at 25°C
Keq at 25°C
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Tertiary Structure of Proteins
Tertiary Structure of Proteins
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Interactions in Protein Folding
Interactions in Protein Folding
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Role of Myoglobin
Role of Myoglobin
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Hydrophobic Collapse
Hydrophobic Collapse
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Protein Folding Process
Protein Folding Process
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Role of Chaperones
Role of Chaperones
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Function of Chaperones
Function of Chaperones
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Amyloidoses
Amyloidoses
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Van der Waals Forces
Van der Waals Forces
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Covalent Bonds in Proteins
Covalent Bonds in Proteins
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Ionic Bonds in Proteins
Ionic Bonds in Proteins
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Function of Proteins
Function of Proteins
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Folding and Environment
Folding and Environment
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Importance of Hydrophilic Residues
Importance of Hydrophilic Residues
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Functions of Nucleic Acids
Functions of Nucleic Acids
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Lipids as Biomolecules
Lipids as Biomolecules
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Study Notes
Hierarchical Organization of a Multicellular Organism
- The human body is composed of 96% H, C, N, and O.
- Elements in biological molecules vary in their abundance.
Biomolecules
- There are 4 major types of biomolecules: amino acids, carbohydrates, lipids, and nucleic acids.
- Amino acids are the building blocks of proteins and have a central carbon atom bonded to an amino group, a carboxyl group, and a variable R group.
Amino Acids
- There are 20 different amino acids, each with a unique R group.
- Amino acids polymerize to form proteins.
- Proteins have a primary structure, which is the sequence of amino acids.
Proteins
- Proteins have a secondary structure, which is the folding of the polypeptide chain.
- Hydrophobic R groups are yellow.
- When the polypeptide chain gets long, folding occurs, resulting in a protein.
- The shape of a protein is critical to its function.
Hydrogen Bonding
- Hydrogen bonds occur between a hydrogen atom in a polar bond and any strongly electronegative atom (usually O or N).
- Hydrogen bonds form between alcohols, aldehydes, ketones, and NH groups.
- It takes about 20 kJ/mol to break hydrogen bonds.
pH and Biochemistry
- pH is an important biochemical parameter.
- The extent of ionization is described by Keq.
- At 25°C, Keq = 1.8 x 10-16 M.
Protein Structure
- Tertiary structure refers to the compact, water-soluble folding of proteins.
- Interactions that dictate protein 3D structure include covalent bonds, ionic bonds, hydrogen bonds, Van der Waals forces, and hydrophobic interactions.
- Many strong and weak interactions stabilize protein 3D structure.
Myoglobin
- Myoglobin illustrates the principles of tertiary structure.
- Hydrophobic residues are clustered inside the protein (stabilized by Van der Waals forces).
- Hydrophilic residues are on the outside of the protein.
Protein Folding
- Protein folding is not a random process.
- Hydrophobic collapse and the formation of secondary structure occur rapidly.
- A series of smaller changes involving fewer residues leads to the acquisition of 3D structure.
Chaperones
- Protein folding is mediated by chaperones.
- Chaperones bind to misfolded proteins, preventing them from sticking together.
- Chaperones release the protein, allowing it to fold and reach its native state.
Amyloidoses
- Amyloidoses are diseases resulting from the formation of protein aggregates, called amyloid fibrils or plaques.
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Description
This quiz covers the basics of biochemistry, focusing on the hierarchical organization of a multicellular organism, particularly the human being. It explores the elements found in biological molecules and their common origin.
